3fy3: Difference between revisions
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==Crystal structure of truncated hemolysin A from P. mirabilis== | |||
=== | <StructureSection load='3fy3' size='340' side='right' caption='[[3fy3]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fy3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FY3 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hpmA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=584 Proteus mirabilis])</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=3fy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fy3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fy3 RCSB], [http://www.ebi.ac.uk/pdbsum/3fy3 PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/3fy3_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this study we analyzed the structure and function of a truncated form of hemolysin A (HpmA265) from Proteus mirabilis using a series of functional and structural studies. Hemolysin A belongs to the two-partner secretion pathway. The two-partner secretion pathway has been identified as the most common protein secretion pathway among Gram-negative bacteria. Currently, the mechanism of action for the two-partner hemolysin members is not fully understood. In this study, hemolysis experiments revealed a unidirectional, cooperative, biphasic activity profile after full-length, inactive hemolysin A was seeded with truncated hemolysin A. We also solved the first x-ray structure of a TpsA hemolysin. The truncated hemolysin A formed a right-handed parallel beta-helix with three adjoining segments of anti-parallel beta-sheet. A CXXC disulfide bond, four buried solvent molecules, and a carboxyamide ladder were all located at the third complete beta-helix coil. Replacement of the CXXC motif led to decreased activity and stability according to hemolysis and CD studies. Furthermore, the crystal structure revealed a sterically compatible, dry dimeric interface formed via anti-parallel beta-sheet interactions between neighboring beta-helix monomers. Laser scanning confocal microscopy further supported the unidirectional interconversion of full-length hemolysin A. From these results, a model has been proposed, where cooperative, beta-strand interactions between HpmA265 and neighboring full-length hemolysin A molecules, facilitated in part by the highly conserved CXXC pattern, account for the template-assisted hemolysis. | |||
Structural and functional studies of truncated hemolysin A from Proteus mirabilis.,Weaver TM, Hocking JM, Bailey LJ, Wawrzyn GT, Howard DR, Sikkink LA, Ramirez-Alvarado M, Thompson JR J Biol Chem. 2009 Aug 14;284(33):22297-309. Epub 2009 Jun 3. PMID:19494116<ref>PMID:19494116</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Hemolysin|Hemolysin]] | *[[Hemolysin|Hemolysin]] | ||
*[[Pore forming toxin%2C | *[[Pore forming toxin%2C ñ-hemolysin|Pore forming toxin%2C ñ-hemolysin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Proteus mirabilis]] | [[Category: Proteus mirabilis]] | ||
[[Category: Bailey, L J | [[Category: Bailey, L J]] | ||
[[Category: Hocking, J M | [[Category: Hocking, J M]] | ||
[[Category: Howard, D R | [[Category: Howard, D R]] | ||
[[Category: Thompson, J R | [[Category: Thompson, J R]] | ||
[[Category: Wawrzyn, G T | [[Category: Wawrzyn, G T]] | ||
[[Category: Weaver, T M | [[Category: Weaver, T M]] | ||
[[Category: Beta helix]] | [[Category: Beta helix]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
Revision as of 14:14, 17 December 2014
Crystal structure of truncated hemolysin A from P. mirabilis
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