5keh: Difference between revisions
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<StructureSection load='5keh' size='340' side='right'caption='[[5keh]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='5keh' size='340' side='right'caption='[[5keh]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5keh]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5keh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KEH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.551Å</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=5keh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5keh OCA], [https://pdbe.org/5keh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5keh RCSB], [https://www.ebi.ac.uk/pdbsum/5keh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5keh ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HLYA_PROMI HLYA_PROMI] | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Proteus mirabilis]] | ||
[[Category: | [[Category: Bhattacharyya B]] | ||
[[Category: | [[Category: Novak WRP]] | ||
[[Category: | [[Category: Weaver TM]] | ||
Latest revision as of 12:59, 27 September 2023
Truncated hemolysin A from P. mirabilis at 2.0 Angstroms resolution crystallized in a high salt conditionTruncated hemolysin A from P. mirabilis at 2.0 Angstroms resolution crystallized in a high salt condition
Structural highlights
FunctionPublication Abstract from PubMedWild-type and variant forms of HpmA265 (truncated hemolysin A) from Proteus mirabilis reveal a right-handed, parallel beta-helix capped and flanked by segments of antiparallel beta-strands. The low-salt crystal structures form a dimeric structure via the implementation of on-edge main-chain hydrogen bonds donated by residues 243-263 of adjacent monomers. Surprisingly, in the high-salt structures of two variants, Y134A and Q125A-Y134A, a new dimeric interface is formed via main-chain hydrogen bonds donated by residues 203-215 of adjacent monomers, and a previously unobserved tetramer is formed. In addition, an eight-stranded antiparallel beta-sheet is formed from the flap regions of crystallographically related monomers in the high-salt structures. This new interface is possible owing to additional proteolysis of these variants after Tyr240. The interface formed in the high-salt crystal forms of hemolysin A variants may mimic the on-edge beta-strand positioning used in template-assisted hemolytic activity. Proteolysis of truncated hemolysin A yields a stable dimerization interface.,Novak WR, Bhattacharyya B, Grilley DP, Weaver TM Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):138-145. doi:, 10.1107/S2053230X17002102. Epub 2017 Feb 21. PMID:28291749[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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