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

Marina Marques Teixeira Vanini, Alberto Spisni, Maurício Luis Sforça, Thelma Aguiar Pertinhez, Celso Eduardo Benedetti

Research output: Contribution to journalArticle

18 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)2051-2064
Number of pages14
JournalProteins: Structure, Function and Genetics
Volume71
Issue number4
DOIs
Publication statusPublished - Jun 2008

Fingerprint

Xanthomonas axonopodis
Lipoproteins
Membranes
Proteins
Citrus
Pathogens
Betaproteobacteria
Gammaproteobacteria
Protein Binding
Scaffolds
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance

Keywords

  • BLIP fold
  • NMR
  • OmlA
  • Outer membrane lipoprotein
  • Protein structure
  • Xanthomonas citri

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

The solution structure of the outer membrane lipoprotein OmIA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction. / Vanini, Marina Marques Teixeira; Spisni, Alberto; Sforça, Maurício Luis; Pertinhez, Thelma Aguiar; Benedetti, Celso Eduardo.

In: Proteins: Structure, Function and Genetics, Vol. 71, No. 4, 06.2008, p. 2051-2064.

Research output: Contribution to journalArticle

Vanini, Marina Marques Teixeira ; Spisni, Alberto ; Sforça, Maurício Luis ; Pertinhez, Thelma Aguiar ; Benedetti, Celso Eduardo. / The solution structure of the outer membrane lipoprotein OmIA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction. In: Proteins: Structure, Function and Genetics. 2008 ; Vol. 71, No. 4. pp. 2051-2064.
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