Structural analysis of substrate binding by the molecular chaperone DnaK. 1996

X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York 10032, USA.

DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D017386 Sequence Homology, Amino Acid The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies

Related Publications

X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
April 2000, Nature structural biology,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
September 2005, Biochemistry,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
January 2001, Biochemical Society symposium,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
May 2003, Biochemistry,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
July 2004, The Journal of biological chemistry,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
October 1995, Gene,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
July 1993, Journal of molecular biology,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
August 2015, Proceedings of the National Academy of Sciences of the United States of America,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
February 1999, Journal of molecular biology,
X Zhu, and X Zhao, and W F Burkholder, and A Gragerov, and C M Ogata, and M E Gottesman, and W A Hendrickson
April 2005, Biochimica et biophysica acta,
Copied contents to your clipboard!