5abk
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5abk]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ABK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ABK FirstGlance]. <br> | <table><tr><td colspan='2'>[[5abk]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ABK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ABK FirstGlance]. <br> | ||
| - | </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=5abk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5abk RCSB], [http://www.ebi.ac.uk/pdbsum/5abk PDBsum]</span></td></tr> | + | </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=5abk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abk OCA], [http://pdbe.org/5abk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5abk RCSB], [http://www.ebi.ac.uk/pdbsum/5abk PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The metalloprotease PrtV from Vibrio cholerae serves an important function for the ability of bacteria to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre-pro-protein that undergoes several N- and C- terminal modifications to form a catalytically active protease. We report here the NMR structure of the PrtV N-terminal domain (residues 23-103) that contains two short alpha-helices in a coiled coil motif. The helices are held together by a cluster of hydrophobic residues. Approximately 30 residues at the C-terminal end, which were predicted to form a third helical structure, are disordered. These residues are highly conserved within the genus Vibrio, which suggests that they might be functionally important. This article is protected by copyright. All rights reserved. | ||
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| + | Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae.,Edwin A, Persson C, Mayzel M, Wai SN, Ohman A, Karlsson BG, Sauer-Eriksson AE Protein Sci. 2015 Oct 5. doi: 10.1002/pro.2815. PMID:26434928<ref>PMID:26434928</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5abk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 23:50, 21 October 2015
Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae
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Categories: Edwin, A | Karlsson, G | Mayzel, M | Ohman, A | Persson, C | Sauer-Eriksson, A E | Wai, S N | Hydrolase | N-terminal domain | Prtv | Vibrio cholerae
