3fy3
From Proteopedia
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| - | {{STRUCTURE_3fy3| PDB=3fy3 | SCENE= }} | ||
| - | ===Crystal structure of truncated hemolysin A from P. mirabilis=== | ||
| - | {{ABSTRACT_PUBMED_19494116}} | ||
| - | == | + | ==Crystal structure of truncated hemolysin A from P. mirabilis== |
| - | [[3fy3]] is a 1 chain structure with sequence from [ | + | <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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3FY3 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]] 1.8Å</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=3fy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fy3 OCA], [https://pdbe.org/3fy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fy3 RCSB], [https://www.ebi.ac.uk/pdbsum/3fy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fy3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HLYA_PROMI HLYA_PROMI] | ||
| + | == 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/initialview03.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/main_output.php?pdb_ID=3fy3 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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 3fy3" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Hemolysin 3D structures|Hemolysin 3D structures]] | ||
| + | *[[Pore forming toxin%2C ñ-hemolysin|Pore forming toxin%2C ñ-hemolysin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Proteus mirabilis]] | [[Category: Proteus mirabilis]] | ||
| - | [[Category: Bailey | + | [[Category: Bailey LJ]] |
| - | [[Category: Hocking | + | [[Category: Hocking JM]] |
| - | [[Category: Howard | + | [[Category: Howard DR]] |
| - | [[Category: Thompson | + | [[Category: Thompson JR]] |
| - | [[Category: Wawrzyn | + | [[Category: Wawrzyn GT]] |
| - | [[Category: Weaver | + | [[Category: Weaver TM]] |
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Current revision
Crystal structure of truncated hemolysin A from P. mirabilis
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