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@article{636664,
author = {Pokorná, Martina and Ciocci, Gianluca and Perret, Stephanie and Rebuffet, Etienne and Kostlánová, Nikola and Adam, Jan and GilboaandGarber, Nechama and Mitchell, Edward P. and Imberty, Anne and Wimmerová, Michaela},
article_location = {USA},
article_number = {24},
keywords = {lectin; microcalorimetry; chromobacterium violaceum; pathogen},
language = {eng},
issn = {0006-2960},
journal = {Biochemistry},
title = {Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose},
volume = {45},
year = {2006}
}
TY - JOUR
ID - 636664
AU - Pokorná, Martina - Ciocci, Gianluca - Perret, Stephanie - Rebuffet, Etienne - Kostlánová, Nikola - Adam, Jan - Gilboa-Garber, Nechama - Mitchell, Edward P. - Imberty, Anne - Wimmerová, Michaela
PY - 2006
TI - Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose
JF - Biochemistry
VL - 45
IS - 24
SP - 7501-7510
EP - 7501-7510
PB - American Chemical Society
SN - 00062960
KW - lectin
KW - microcalorimetry
KW - chromobacterium violaceum
KW - pathogen
N2 - 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 preference for fucose. We describe here the cloning of CV-IIL and its expression as a recombinant protein. A complete structure-function characterization has been made in an effort to analyze the specificity and affinity of CV-IIL for fucose and mannose. Crystal structures of CV-IIL complexes with monosaccharides have yielded the molecular basis of the specificity. Each monomer contains two close calcium cations that mediate the binding of the monosaccharides, which occurs in different orientations for fucose and mannose. The thermodynamics of binding has been analyzed by titration microcalorimetry, giving dissociation constants of 1.7 and 19 íM for R-methyl fucoside and R-methyl mannoside, respectively. Further analysis demonstrated a strongly favorable entropy term that is unusual in carbohydrate binding. A comparison with both PA-IIL and RS-IIL, which have binding preferences for fucose and mannose, respectively, yielded insights into the monosaccharide specificity of this important class of soluble bacterial lectins.
ER -
POKORNÁ, Martina, Gianluca CIOCCI, Stephanie PERRET, Etienne REBUFFET, Nikola KOSTLÁNOVÁ, Jan ADAM, Nechama GILBOA-GARBER, Edward P. MITCHELL, Anne IMBERTY and Michaela WIMMEROVÁ. Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose. \textit{Biochemistry}. USA: American Chemical Society, 2006, vol.~45, No~24, p.~7501-7510. ISSN~0006-2960.
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