Publications
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The Bacillus subtilis RNA helicase YxiN is distended in solution.
Wang S,
Overgaard MT, Hu Y, McKay DB.
Biophys J.
2008;
94
(1):
L01-3
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The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.
Xu X,
Wang S, Hu YX, McKay DB.
J Mol Biol.
2007;
373
(2):
367-81
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Retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation.
Caruthers JM,
Feng Y, McKay DB, Cohen SN.
J Biol Chem.
2006;
281
(37):
27046-51
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Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription.
Wang S,
Fleming RT, Westbrook EM, Matsumura P, McKay DB.
J Mol Biol.
2006;
355
(4):
798-808
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Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN.
Caruthers JM,
Hu Y, McKay DB.
Acta Crystallogr Sect F Struct Biol Cryst Commun.
2006;
62
(Pt 12):
1191-5
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The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold.
Wang S,
Hu Y, Overgaard MT, Karginov FV, Uhlenbeck OC, McKay DB.
RNA.
2006;
12
(6):
959-67
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YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain.
Karginov FV,
Caruthers JM, Hu Y, McKay DB, Uhlenbeck OC.
J Biol Chem.
2005;
280
(42):
35499-505
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Kinetics of protein substrate degradation by HslUV.
Kwon AR,
Trame CB, McKay DB.
J Struct Biol.
2004 Apr-May;
146
(1-2):
141-7
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Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins.
Bitto E,
McKay DB.
FEBS Lett.
2004;
568
(1-3):
94-8
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Crystal structure of the leadzyme at 1.8 A resolution: metal ion binding and the implications for catalytic mechanism and allo site ion regulation.
Wedekind JE,
McKay DB.
Biochemistry.
2003;
42
(32):
9554-63
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Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome.
Kwon AR,
Kessler BM, Overkleeft HS, McKay DB.
J Mol Biol.
2003;
330
(2):
185-95
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Structure of the Yersinia enterocolitica molecular-chaperone protein SycE.
Trame CB,
McKay DB.
Acta Crystallogr D Biol Crystallogr.
2003;
59
(Pt 2):
389-92
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The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.
Bitto E,
McKay DB.
J Biol Chem.
2003;
278
(49):
49316-22
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Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU.
Sousa MC,
Kessler BM, Overkleeft HS, McKay DB.
J Mol Biol.
2002;
318
(3):
779-85
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Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.
Bitto E,
McKay DB.
Structure.
2002;
10
(11):
1489-98
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Helicase structure and mechanism.
Caruthers JM,
McKay DB.
Curr Opin Struct Biol.
2002;
12
(1):
123-33
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Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity.
Wedekind JE,
Trame CB, Dorywalska M, Koehl P, Raschke TM, McKee M, FitzGerald D, Collier RJ, McKay DB.
J Mol Biol.
2001;
314
(4):
823-37
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Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning.
Trame CB,
McKay DB.
Acta Crystallogr D Biol Crystallogr.
2001;
57
(Pt 8):
1079-90
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Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.
Sousa MC,
McKay DB.
Acta Crystallogr D Biol Crystallogr.
2001;
57
(Pt 12):
1950-4
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Structure of the universal stress protein of Haemophilus influenzae.
Sousa MC,
McKay DB.
Structure.
2001;
9
(12):
1135-41
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Crystal and solution structures of an HslUV protease-chaperone complex.
Sousa MC,
Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB.
Cell.
2000;
103
(4):
633-43
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Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase.
Caruthers JM,
Johnson ER, McKay DB.
Proc Natl Acad Sci U S A.
2000;
97
(24):
13080-5
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Purification, crystallization, and X-ray diffraction analysis of small ribozymes.
Wedekind JE,
McKay DB.
Methods Enzymol.
2000:
317
149-68
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Crystal structure of a lead-dependent ribozyme revealing metal binding sites relevant to catalysis.
Wedekind JE,
McKay DB.
Nat Struct Biol.
1999;
6
(3):
261-8
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Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase.
Johnson ER,
McKay DB.
RNA.
1999;
5
(12):
1526-34
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Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein.
Johnson ER,
McKay DB.
Biochemistry.
1999;
38
(33):
10823-30
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Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis.
Wedekind JE,
McKay DB.
Annu Rev Biophys Biomol Struct.
1998:
27
475-502
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Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70.
Wilbanks SM,
McKay DB.
Biochemistry.
1998;
37
(20):
7456-62
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The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change.
Sousa MC,
McKay DB.
Biochemistry.
1998;
37
(44):
15392-9
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Destabilization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone.
Ha JH,
Hellman U, Johnson ER, Li L, McKay DB, Sousa MC, Takeda S, Wernstedt C, Wilbanks SM.
J Biol Chem.
1997;
272
(44):
27796-803
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Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone.
Takeda S,
McKay DB.
Biochemistry.
1996;
35
(14):
4636-44
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Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis.
O'Brien MC,
Flaherty KM, McKay DB.
J Biol Chem.
1996;
271
(27):
15874-8
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Structure and function of the hammerhead ribozyme: an unfinished story.
McKay DB,
RNA.
1996;
2
(5):
395-403
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How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity.
O'Brien MC,
McKay DB.
J Biol Chem.
1995;
270
(5):
2247-50
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How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site.
Wilbanks SM,
McKay DB.
J Biol Chem.
1995;
270
(5):
2251-7
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Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding.
Ha JH,
McKay DB.
Biochemistry.
1995;
34
(36):
11635-44
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Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments.
Wilbanks SM,
Chen L, Tsuruta H, Hodgson KO, McKay DB.
Biochemistry.
1995;
34
(38):
12095-106
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ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain.
Ha JH,
McKay DB.
Biochemistry.
1994;
33
(48):
14625-35
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Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix.
Pley HW,
Flaherty KM, McKay DB.
Nature.
1994;
372
(6501):
111-3
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Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants.
Wilbanks SM,
DeLuca-Flaherty C, McKay DB.
J Biol Chem.
1994;
269
(17):
12893-8
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Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.
Flaherty KM,
Wilbanks SM, DeLuca-Flaherty C, McKay DB.
J Biol Chem.
1994;
269
(17):
12899-907
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Three-dimensional structure of a hammerhead ribozyme.
Pley HW,
Flaherty KM, McKay DB.
Nature.
1994;
372
(6501):
68-74
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Crystals of a hammerhead ribozyme.
Pley HW,
Lindes DS, DeLuca-Flaherty C, McKay DB.
J Biol Chem.
1993;
268
(26):
19656-8
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Structure and mechanism of 70-kDa heat-shock-related proteins.
McKay DB,
Adv Protein Chem.
1993:
44
67-98
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Three-dimensional structure of recoverin, a calcium sensor in vision.
Flaherty KM,
Zozulya S, Stryer L, McKay DB.
Cell.
1993;
75
(4):
709-16
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Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif.
Baumann U,
Wu S, Flaherty KM, McKay DB.
EMBO J.
1993;
12
(9):
3357-64
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Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis.
O'Brien MC,
McKay DB.
J Biol Chem.
1993;
268
(32):
24323-9
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Cloning, expression, and crystallization of recoverin, a calcium sensor in vision.
Ray S,
Zozulya S, Niemi GA, Flaherty KM, Brolley D, Dizhoor AM, McKay DB, Hurley J, Stryer L.
Proc Natl Acad Sci U S A.
1992;
89
(13):
5705-9
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Crystallographic structures of the elastase of Pseudomonas aeruginosa.
McKay DB,
Thayer MM, Flaherty KM, Pley H, Benvegnu D.
Matrix Suppl.
1992:
1
112-5
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Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein.
Flaherty KM,
McKay DB, Kabsch W, Holmes KC.
Proc Natl Acad Sci U S A.
1991;
88
(11):
5041-5
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Structure of the 70-kilodalton heat-shock-related proteins.
McKay DB,
Springer Semin Immunopathol.
1991;
13
(1):
1-9
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Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock cognate protein.
DeLuca-Flaherty C,
McKay DB.
Nucleic Acids Res.
1990;
18
(18):
5569
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Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein.
Flaherty KM,
DeLuca-Flaherty C, McKay DB.
Nature.
1990;
346
(6285):
623-8
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Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis.
DeLuca-Flaherty C,
McKay DB, Parham P, Hill BL.
Cell.
1990;
62
(5):
875-87
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