2pxg
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(New page: 200px<br /><applet load="2pxg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pxg" /> '''NMR Solution Structure of OmlA'''<br /> ==O...)
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Revision as of 08:58, 31 January 2008
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NMR Solution Structure of OmlA
Overview
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.
About this Structure
2PXG is a Single protein structure of sequence from Xanthomonas axonopodis pv. citri. Full crystallographic information is available from OCA.
Reference
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
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