A specific interdomain interaction preserves the structural and binding properties of the ModA protein from the phytopathogen Xanthomonas citri domain interaction and transport in ModA-Reference-Cited by-同舟云学术

A specific interdomain interaction preserves the structural and binding properties of the ModA protein from the phytopathogen Xanthomonas citri domain interaction and transport in ModA

Published:2013-11 Issue:1 Volume:539 Page:20-30
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Santacruz-Perez Carolina,Pegos Vanessa Rodrigues,Honorato Rodrigo V.,Verli Hugo,Lindahl Erik,Barbosa João Alexandre Ribeiro Gonçalves,Balan Andrea

Funder

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Associação Brasileira de Tecnologia de Luz Síncrotron (ABTLuS)

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference56 articles.

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5. The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins.

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The periplasmic binding protein NrtT affects xantham gum production and pathogenesis in Xanthomonas citri;FEBS Open Bio;2017-09-13

2. Structure determination of a sugar-binding protein from the phytopathogenic bacteriumXanthomonas citri;Acta Crystallographica Section F Structural Biology Communications;2014-04-17