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|1dkz, resolution 2.00Å ()|
THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 NATIVE CRYSTALS
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.
Structural analysis of substrate binding by the molecular chaperone DnaK., Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA, Science. 1996 Jun 14;272(5268):1606-14. PMID:8658133
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1dkz is a 2 chain structure with sequence from Escherichia coli. The August 2002 RCSB PDB Molecule of the Month feature on Chaperones by David S. Goodsell is 10.2210/rcsb_pdb/mom_2002_8. Full crystallographic information is available from OCA.
- Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA. Structural analysis of substrate binding by the molecular chaperone DnaK. Science. 1996 Jun 14;272(5268):1606-14. PMID:8658133
- Galkin A, Sarikaya E, Lehmann C, Howard A, Herzberg O. X-ray structure of HI0817 from Haemophilus influenzae: protein of unknown function with a novel fold. Proteins. 2004 Dec 1;57(4):874-7. PMID:15317022 doi:10.1002/prot.20260