4jnf: Difference between revisions
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<StructureSection load='4jnf' size='340' side='right'caption='[[4jnf]], [[Resolution|resolution]] 1.62Å' scene=''> | <StructureSection load='4jnf' size='340' side='right'caption='[[4jnf]], [[Resolution|resolution]] 1.62Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jnf]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JNF FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnf OCA], [https://pdbe.org/4jnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jnf RCSB], [https://www.ebi.ac.uk/pdbsum/4jnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnf ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hendrickson | [[Category: Hendrickson WA]] | ||
[[Category: Le | [[Category: Le KQ]] | ||
[[Category: Liu | [[Category: Liu Q]] | ||
[[Category: Qi | [[Category: Qi R]] | ||
[[Category: Sarbeng | [[Category: Sarbeng EB]] | ||
[[Category: Vorvis | [[Category: Vorvis C]] | ||
[[Category: Wong | [[Category: Wong JL]] | ||
[[Category: Xu | [[Category: Xu H]] | ||
[[Category: Xu | [[Category: Xu X]] | ||
[[Category: Yang | [[Category: Yang J]] | ||
[[Category: Zhou | [[Category: Zhou L]] | ||
Revision as of 14:25, 24 November 2022
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATPAllosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
Structural highlights
FunctionDNAK_ECOLI Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332] Publication Abstract from PubMedThe 70-kilodalton (kDa) heat-shock proteins (Hsp70s) are ubiquitous molecular chaperones essential for cellular protein folding and proteostasis. Each Hsp70 has two functional domains: a nucleotide-binding domain (NBD), which binds and hydrolyzes ATP, and a substrate-binding domain (SBD), which binds extended polypeptides. NBD and SBD interact little when in the presence of ADP; however, ATP binding allosterically couples the polypeptide- and ATP-binding sites. ATP binding promotes polypeptide release; polypeptide rebinding stimulates ATP hydrolysis. This allosteric coupling is poorly understood. Here we present the crystal structure of an intact ATP-bound Hsp70 from Escherichia coli at 1.96-A resolution. The ATP-bound NBD adopts a unique conformation, forming extensive interfaces with an SBD that has changed radically, having its alpha-helical lid displaced and the polypeptide-binding channel of its beta-subdomain restructured. These conformational changes, together with our biochemical assays, provide a structural explanation for allosteric coupling in Hsp70 activity. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP.,Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, Xu H, Yang J, Wong JL, Vorvis C, Hendrickson WA, Zhou L, Liu Q Nat Struct Mol Biol. 2013 Jul;20(7):900-7. doi: 10.1038/nsmb.2583. Epub 2013 May , 26. PMID:23708608[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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