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@article{491728,
author = {Sudakevitz, Dvora and Kostlánová, Nikola and BlatmanandJan, Gittit and Mitchell, Edward P. and Lerrer, Batia and Wimmerová, Michaela and Katcoff, Don J. and Imberty, Anne and GilboaandGarber, Nechama},
article_number = {3},
keywords = {ralstonia solanacearum; lectin; crystal structure; plant pathogen},
language = {eng},
issn = {0950-382X},
journal = {Molecular Microbiology},
title = {A new Ralstonia solanacearum high affinity mannose-binding lectin},
volume = {52},
year = {2004}
}
TY - JOUR
ID - 491728
AU - Sudakevitz, Dvora - Kostlánová, Nikola - Blatman-Jan, Gittit - Mitchell, Edward P. - Lerrer, Batia - Wimmerová, Michaela - Katcoff, Don J. - Imberty, Anne - Gilboa-Garber, Nechama
PY - 2004
TI - A new Ralstonia solanacearum high affinity mannose-binding lectin
JF - Molecular Microbiology
VL - 52
IS - 3
SP - 691-700
EP - 691-700
PB - Blackwell Publishing Ltd
SN - 0950382X
KW - ralstonia solanacearum
KW - lectin
KW - crystal structure
KW - plant pathogen
N2 - The plant pathogen Ralstonia solanacearum produces two lectins, each with different affinity for fucose. We described previously the properties and sequence of the first lectin, RSL (subunit Mr 9.9 kDa), that 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 Mr 11.6 kDa), a tetrameric lectin, with high sequence similarity to the fucose-binding lectin PA-IIL of Pseudomanas 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 et al. (2002) Nature Struct. Biol. 9: 918-921). Each monomer contains two close calcium cations which 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 while the preference for mannose versus fucose can be attributed to the change of a three amino acids sequence in the "specificity loop".
ER -
SUDAKEVITZ, Dvora, Nikola KOSTLÁNOVÁ, Gittit BLATMAN-JAN, Edward P. MITCHELL, Batia LERRER, Michaela WIMMEROVÁ, Don J. KATCOFF, Anne IMBERTY and Nechama GILBOA-GARBER. A new Ralstonia solanacearum high affinity mannose-binding lectin. \textit{Molecular Microbiology}. Blackwell Publishing Ltd, 2004, vol.~52, No~3, p.~691-700. ISSN~0950-382X.
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