5ycq
From Proteopedia
(Difference between revisions)
m (Protected "5ycq" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Unique Specificity-Enhancing Factor for the AAA+ Lon Protease== | |
| + | <StructureSection load='5ycq' size='340' side='right' caption='[[5ycq]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ycq]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vbv 1vbv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YCQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ycq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycq OCA], [http://pdbe.org/5ycq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ycq RCSB], [http://www.ebi.ac.uk/pdbsum/5ycq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HSPQ_ECO55 HSPQ_ECO55]] Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The heat shock protein HspQ (YccV) of Escherichia coli has been proposed to participate in the retardation of replication initiation in cells with the dnaA508 allele. In this study, we have determined the 2.5-A-resolution X-ray structure of the trimer of HspQ, which is also the first structure of a member of the YccV superfamily. The acidic character of the HspQ trimer suggests an interaction surface with basic proteins. From these results, we discuss the cellular function of HspQ, including its relationship with the DnaA508 protein. | ||
| - | + | X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation.,Abe Y, Shioi S, Kita S, Nakata H, Maenaka K, Kohda D, Katayama T, Ueda T FEBS Lett. 2017 Nov;591(22):3805-3816. doi: 10.1002/1873-3468.12892. Epub 2017, Nov 12. PMID:29083032<ref>PMID:29083032</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ycq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Abe, Y]] | ||
| + | [[Category: Katayama, T]] | ||
| + | [[Category: Kita, S]] | ||
| + | [[Category: Kohda, D]] | ||
| + | [[Category: Maenaka, K]] | ||
| + | [[Category: Nakata, H]] | ||
| + | [[Category: Shioi, S]] | ||
| + | [[Category: Ueda, T]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Heat shock protein]] | ||
Revision as of 13:40, 11 April 2018
Unique Specificity-Enhancing Factor for the AAA+ Lon Protease
| |||||||||||
Categories: Abe, Y | Katayama, T | Kita, S | Kohda, D | Maenaka, K | Nakata, H | Shioi, S | Ueda, T | Dna binding protein | Heat shock protein
