View source for 5kf3


==Truncated hemolysin A from P. mirabilis Y134A at 2.2 Angstroms resolution==
<StructureSection load='5kf3' size='340' side='right'caption='[[5kf3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kf3]] 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=5KF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KF3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=5kf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kf3 OCA], [https://pdbe.org/5kf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kf3 RCSB], [https://www.ebi.ac.uk/pdbsum/5kf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kf3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HLYA_PROMI HLYA_PROMI] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kf3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Proteus mirabilis]]
[[Category: Bhattacharyya B]]
[[Category: Novak WRP]]
[[Category: Weaver TM]]