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| [[Image:1dky.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1dky| PDB=1dky | SCENE= }} | | {{STRUCTURE_1dky| PDB=1dky | SCENE= }} |
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| '''THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS'''
| | ===THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8658133}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8658133 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8658133}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zhu, X.]] | | [[Category: Zhu, X.]] |
| [[Category: Dnak]] | | [[Category: Dnak]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:58:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:13:35 2008'' |
