This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2xuv
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==The structure of HdeB== | ==The structure of HdeB== | ||
| - | <StructureSection load='2xuv' size='340' side='right' caption='[[2xuv]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='2xuv' size='340' side='right'caption='[[2xuv]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2xuv]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2xuv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XUV FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2xuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xuv OCA], [https://pdbe.org/2xuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xuv RCSB], [https://www.ebi.ac.uk/pdbsum/2xuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xuv ProSAT]</span></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| + | [https://www.uniprot.org/uniprot/HDEB_ECOLI HDEB_ECOLI] Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.<ref>PMID:17085547</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 14: | Line 16: | ||
Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone Function.,Wang W, Rasmussen T, Harding AJ, Booth NA, Booth IR, Naismith JH J Mol Biol. 2011 Nov 25. PMID:22138344<ref>PMID:22138344</ref> | Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone Function.,Wang W, Rasmussen T, Harding AJ, Booth NA, Booth IR, Naismith JH J Mol Biol. 2011 Nov 25. PMID:22138344<ref>PMID:22138344</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | <div class="pdbe-citations 2xuv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 21: | Line 24: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Naismith JH]] |
| - | [[Category: | + | [[Category: Wang W]] |
Current revision
The structure of HdeB
| |||||||||||
