5kf3
From Proteopedia
(Difference between revisions)
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<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=5kf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kf3 OCA], [http://pdbe.org/5kf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kf3 RCSB], [http://www.ebi.ac.uk/pdbsum/5kf3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kf3 ProSAT]</span></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=5kf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kf3 OCA], [http://pdbe.org/5kf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kf3 RCSB], [http://www.ebi.ac.uk/pdbsum/5kf3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kf3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Wild-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. | ||
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| + | 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<ref>PMID:28291749</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5kf3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:59, 17 May 2017
Truncated hemolysin A from P. mirabilis Y134A at 2.2 Angstroms resolution
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