2pxg
From Proteopedia
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| - | [[Image:2pxg.jpg|left|200px]] | ||
| - | < | + | ==NMR Solution Structure of OmlA== |
| - | + | <StructureSection load='2pxg' size='340' side='right'caption='[[2pxg]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2pxg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PXG FirstGlance]. <br> | |
| - | + | </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=2pxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pxg OCA], [https://pdbe.org/2pxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pxg RCSB], [https://www.ebi.ac.uk/pdbsum/2pxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pxg ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q8PMB6_XANAC Q8PMB6_XANAC] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (By similarity).[HAMAP-Rule:MF_00925] | |
| - | + | == 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/px/2pxg_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/main_output.php?pdb_ID=2pxg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The outer membrane lipoprotein A (OmlA) belongs to a family of bacterial small lipoproteins widely distributed across the beta and gamma proteobacteria. Although the role of numerous bacterial lipoproteins is known, the biological function of OmlA remains elusive. We found that in the citrus canker pathogen, Xanthomonas axonopodis pv. citri (X. citri), OmlA is coregulated with the ferric uptake regulator (Fur) and their expression is enhanced when X. citri is grown on citrus leaves, suggesting that these proteins are involved in plant-pathogen interaction. To gain insights into the function of OmlA, its conformational and dynamic features were determined by nuclear magnetic resonance. The protein has highly flexible N- and C- termini and a structurally well defined core composed of three beta-strands and two small alpha-helices, which pack against each other forming a two-layer alpha/beta scaffold. This protein fold resembles the domains of the beta-lactamase inhibitory protein BLIP, involved in protein-protein binding. In conclusion, the structure of OmlA does suggest that this protein may be implicated in protein-protein interactions required during X. citri infection. Proteins 2008. (c) 2008 Wiley-Liss, Inc. | The outer membrane lipoprotein A (OmlA) belongs to a family of bacterial small lipoproteins widely distributed across the beta and gamma proteobacteria. Although the role of numerous bacterial lipoproteins is known, the biological function of OmlA remains elusive. We found that in the citrus canker pathogen, Xanthomonas axonopodis pv. citri (X. citri), OmlA is coregulated with the ferric uptake regulator (Fur) and their expression is enhanced when X. citri is grown on citrus leaves, suggesting that these proteins are involved in plant-pathogen interaction. To gain insights into the function of OmlA, its conformational and dynamic features were determined by nuclear magnetic resonance. The protein has highly flexible N- and C- termini and a structurally well defined core composed of three beta-strands and two small alpha-helices, which pack against each other forming a two-layer alpha/beta scaffold. This protein fold resembles the domains of the beta-lactamase inhibitory protein BLIP, involved in protein-protein binding. In conclusion, the structure of OmlA does suggest that this protein may be implicated in protein-protein interactions required during X. citri infection. Proteins 2008. (c) 2008 Wiley-Liss, Inc. | ||
| - | + | The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction.,Vanini MM, Spisni A, Sforca ML, Pertinhez TA, Benedetti CE Proteins. 2008 Jan 10;. PMID:18186471<ref>PMID:18186471</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2pxg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Xanthomonas | + | == References == |
| - | [[Category: Benedetti | + | <references/> |
| - | [[Category: Pertinhez | + | __TOC__ |
| - | [[Category: Sforca | + | </StructureSection> |
| - | [[Category: Spisni | + | [[Category: Large Structures]] |
| - | [[Category: Vanini | + | [[Category: Xanthomonas citri]] |
| - | + | [[Category: Benedetti CE]] | |
| - | + | [[Category: Pertinhez TA]] | |
| - | + | [[Category: Sforca ML]] | |
| - | + | [[Category: Spisni A]] | |
| + | [[Category: Vanini MMT]] | ||
Current revision
NMR Solution Structure of OmlA
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