Structural analysis of substrate binding by the molecular chaperone DnaK

Science

Volumn 272, Issue 5268, 1996, Pages 1606-1614

  Zhu, Xiaotian ^a,b   Zhao, Xun ^a   Burkholder, William F ^a,b   Gragerov, Alexander ^a,d   Ogata, Craig M ^c   Gottesman, Max E ^a,b   Hendrickson, Wayne A ^a,b  

^a Columbia University ^*  (United States)

^b Och Spine at New York Presbyterian Hospitals   (United States)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^d NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE;

EID: 0029937037     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5268.1606     Document Type: Article

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71. We thank Y. Liu for help in synchrotron data collection; F. Athappilly for his help in crystallization of selenomethionyl DnaK by dialysis; M. Gawinowitz for amino-acid sequencing; N. Pileggi for synthesis of selenomethionyl peptides; D. King and B. Pramanik for mass spectrometric data; and laboratory colleagues for discussion, especially C. Lima, Y. Liu, L. Shapiro, P. Kwong, H. Wu, D. Fremont, and X. Jiang. Supported in part by NIH grants GM34102 (W.A.H.) and GM37219 (M.E.G.). Beamline X4A at the National Synchrotron Light Source, a Department of Energy facility, is supported by the Howard Hughes Medical Institute. The coordinates have been deposited in PDB (1DKX, 1DKY, and 1DKZ).