1uqx
From Proteopedia
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Revision as of 14:03, 30 October 2007
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RALSTONIA SOLANACEARUM LECTIN (RS-IIL) IN COMPLEX WITH ALPHA-METHYLMANNOSIDE
Overview
The plant pathogen Ralstonia solanacearum produces two lectins, each with, different affinity to fucose. We described previously the properties and, sequence of the first lectin, RSL (subunit M(r) 9.9 kDa), which is related, to fungal lectins (Sudakevitz, D., Imberty, A., and Gilboa-Garber, N., 2002, J Biochem 132: 353-358). The present communication reports the, discovery of the second one, RS-IIL (subunit M(r) 11.6 kDa), a tetrameric, lectin, with high sequence similarity to the fucose-binding lectin PA-IIL, of Pseudomonas aeruginosa. RS-IIL recognizes fucose but displays much, higher affinity to mannose and fructose, which is opposite to the, preference spectrum of PA-IIL. Determination of the crystal structure of, RS-IIL complexed with a mannose derivative demonstrates a tetrameric, ... [(full description)]
About this Structure
1UQX is a [Single protein] structure of sequence from [Ralstonia solanacearum] with MMA and CA as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
A new Ralstonia solanacearum high-affinity mannose-binding lectin RS-IIL structurally resembling the Pseudomonas aeruginosa fucose-specific lectin PA-IIL., Sudakevitz D, Kostlanova N, Blatman-Jan G, Mitchell EP, Lerrer B, Wimmerova M, Katcoff DJ, Imberty A, Gilboa-Garber N, Mol Microbiol. 2004 May;52(3):691-700. PMID:15101976
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