2PXG

NMR Solution Structure of OmlA

Summary for 2PXG

• Entry DOI: 10.2210/pdb2pxg/pdb
• NMR Information: BMRB: 6797
• Descriptor: Outer membrane protein (1 entity in total)
• Functional Keywords: two layer alpha/beta plait, two layer sandwich architecture, membrane protein
• Biological source: Xanthomonas axonopodis pv. citri
• Total number of polymer chains: 1
• Total formula weight: 13602.29

Authors

Vanini, M.M.T.,Pertinhez, T.A.,Sforca, M.L.,Spisni, A.,Benedetti, C.E. (deposition date: 2007-05-14, release date: 2008-01-29, Last modification date: 2024-05-15)

Primary citation

Vanini, M.M.,Spisni, A.,Sforca, M.L.,Pertinhez, T.A.,Benedetti, C.E.
The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction.
Proteins, 71:2051-2064, 2008

PubMed Abstract: 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.

PubMed: 18186471
DOI: 10.1002/prot.21886

Experimental method

SOLUTION NMR