1dkz
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1dkz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkz, resolution 2.0Å" /> '''THE SUBSTRATE BINDIN...)
Next diff →
Revision as of 06:52, 18 November 2007
|
THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 NATIVE CRYSTALS
Overview
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.
About this Structure
1DKZ is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1DKZ with [Chaperones]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Nov 18 08:58:59 2007
