2bv4

From Proteopedia

Revision as of 10:57, 30 October 2007

1.0A STRUCTURE OF CHROMOBACTERIUM VIOLACEUM LECTIN IN COMPLEX WITH ALPHA-METHYL-MANNOSIDE

Overview

The purple pigmented bacterium Chromobacterium violaceum is a dominant, component of tropical soil microbiota that can cause rare but fatal, septicaemia in humans. Its sequenced genome provides insight into the, abundant potential of this organism for biotechnological and, pharmaceutical applications and allowed an ORF encoding a protein that is, 60% identical to the fucose binding lectin (PA-IIL) from Pseudomonas, aeruginosa and the mannose binding lectin (RS-IIL) from Ralstonia, solanacearum to be identified. The lectin, CV-IIL, has recently been, purified from C. violaceum [Zinger-Yosovich, K., Sudakevitz, D., Imberty, A., Garber, N. C., and Gilboa-Garber, N. (2006) Microbiology 152, 457-463], and has been confirmed to be a tetramer with subunit size of 11.86 kDa and, a binding ... [(full description)]

About this Structure

2BV4 is a [Single protein] structure of sequence from [Chromobacterium violaceum] with MMA and CA as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Unusual entropy-driven affinity of Chromobacterium violaceum lectin CV-IIL toward fucose and mannose., Pokorna M, Cioci G, Perret S, Rebuffet E, Kostlanova N, Adam J, Gilboa-Garber N, Mitchell EP, Imberty A, Wimmerova M, Biochemistry. 2006 Jun 20;45(24):7501-10. PMID:16768446

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