Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri


Autoria(s): BALAN, Andrea; SANTACRUZ-PEREZ, Carolina; MOUTRAN, Alexandre; FERREIRA, Luis Carlos Souza; NESHICH, Goran; BARBOSA, Joao Alexandre Ribeiro Goncalves
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

20/10/2012

20/10/2012

2008

Resumo

In Xanthomonas axonopodis pv. citri (Xac or X citri), the modA gene codes for a periplasmic protein (ModA) that is capable of binding molybdate and tungstate as part of the ABC-type transporter required for the uptake of micronutrients. In this study, we report the crystallographic structure of the Xac ModA protein with bound molybdate. The Xac ModA structure is similar to orthologs with known three-dimensional structures and consists of two nearly symmetrical domains separated by a hinge region where the oxyanion-binding site lies. Phylogenetic analysis of different ModA orthologs based on sequence alignments revealed three groups of molybdate-binding proteins: bacterial phytopathogens, enterobacteria and soil bacteria. Even though the ModA orthologs are segregated into different groups, the ligand-binding hydrogen bonds are mostly conserved, except for Archaeglobus fulgidus ModA. A detailed discussion of hydrophobic interactions in the active site is presented and two new residues, Ala(38) and Ser(151), are shown to be part of the ligand-binding pocket. (c) 2007 Elsevier B.V All rights reserved.

Identificador

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v.1784, n.2, p.393-399, 2008

1570-9639

http://producao.usp.br/handle/BDPI/28643

10.1016/j.bbapap.2007.11.013

http://dx.doi.org/10.1016/j.bbapap.2007.11.013

Idioma(s)

eng

Publicador

ELSEVIER SCIENCE BV

Relação

Biochimica Et Biophysica Acta-proteins and Proteomics

Direitos

restrictedAccess

Copyright ELSEVIER SCIENCE BV

Palavras-Chave #ModA #molybdate-binding protein #Xanthomonas axonopodis pv. citri #ABC transporters #X-ray crystal structure #ESCHERICHIA-COLI #CRYSTAL-STRUCTURE #TRANSPORT OPERON #MODA #MOLYBDENUM #SPECIFICITY #RECEPTORS #TUNGSTATE #ALIGNMENT #BACTERIA #Biochemistry & Molecular Biology #Biophysics
Tipo

article

original article

publishedVersion