2chh: Difference between revisions

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==Overview==
==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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15101976 (full description)]]
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, structure very similar to the recently solved PA-IIL structure (Mitchell, E., et al., 2002, Nature Struct Biol 9: 918-921). Each monomer contains, two close calcium cations that mediate the binding of the monosaccharide, and explain the outstandingly high affinity to the monosaccharide ligand., The binding loop of the cations is fully conserved in RS-IIL and PA-IIL, whereas the preference for mannose versus fucose can be attributed to the, change of a three-amino-acid sequence in the 'specificity loop'.


==About this Structure==
==About this Structure==
2CHH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Ralstonia_solanacearum Ralstonia solanacearum]] with CA and UNX as [[http://en.wikipedia.org/wiki/ligands ligands]]. This structure superseeds the now removed PDB entry 1VYY. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHH OCA]].  
2CHH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ralstonia_solanacearum Ralstonia solanacearum] with CA and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1VYY. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHH OCA].  


==Reference==
==Reference==
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[[Category: sugar-binding protein]]
[[Category: sugar-binding protein]]


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