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2pxg

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Revision as of 18:31, 20 October 2021

NMR Solution Structure of OmlA

Structural highlights

2pxg is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vanini MM, Spisni A, Sforca ML, Pertinhez TA, Benedetti CE. The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction. Proteins. 2008 Jan 10;. PMID:18186471 doi:10.1002/prot.21886

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pxg"

@@ Line 3: / Line 3: @@
 <StructureSection load='2pxg' size='340' side='right'caption='[[2pxg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pxg]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PXG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pxg]] is a 1 chain structure. 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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pxg OCA], [http://pdbe.org/2pxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pxg RCSB], [http://www.ebi.ac.uk/pdbsum/2pxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pxg ProSAT]</span></td></tr>
+</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 ==
-[[http://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]
+[[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]]

2pxg

From Proteopedia

Revision as of 18:31, 20 October 2021

NMR Solution Structure of OmlA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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