DOI: 10.1002/prot.21886. The solution structure of the outer membrane lipoprotein OmlA from <i>Xanthomonas axonopodis</i> pv. <i>citri</i> reveals a protein fold implicated in protein

The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein–protein interaction

10.1002/prot.21886

Crossref journal-article

Wiley

Proteins: Structure, Function, and Bioinformatics (311)

Abstract

AbstractThe 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 β‐strands and two small α‐helices, which pack against each other forming a two‐layer alpha/beta scaffold. This protein fold resembles the domains of the β‐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. © 2008 Wiley‐Liss, Inc.

Bibliography

Vanini, M. M. T., Spisni, A., SforÃ§a, M. L., Pertinhez, T. A., & Benedetti, C. E. (2008). The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in proteinâprotein interaction. Proteins: Structure, Function, and Bioinformatics, 71(4), 2051â2064. Portico.

Authors 5

Marina Marques Teixeira Vanini (first)
Alberto Spisni (additional)
Maurício Luis Sforça (additional)
Thelma Aguiar Pertinhez (additional)
Celso Eduardo Benedetti (additional)

References 60 Referenced 19

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Dates

Type	When
Created	17 years, 7 months ago (Jan. 10, 2008, 1:17 p.m.)
Deposited	1 year, 10 months ago (Oct. 9, 2023, 3:38 p.m.)
Indexed	4 months ago (April 30, 2025, 4:43 a.m.)
Issued	17 years, 7 months ago (Jan. 10, 2008)
Published	17 years, 7 months ago (Jan. 10, 2008)
Published Online	17 years, 7 months ago (Jan. 10, 2008)
Published Print	17 years, 3 months ago (June 1, 2008)

Funders 0

None

BibTeX

@article{Vanini_2008, title={The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein–protein interaction}, volume={71}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.21886}, DOI={10.1002/prot.21886}, number={4}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Vanini, Marina Marques Teixeira and Spisni, Alberto and Sforça, Maurício Luis and Pertinhez, Thelma Aguiar and Benedetti, Celso Eduardo}, year={2008}, month=jan, pages={2051–2064} }

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