Binding of different monosaccharides by lectin PA-IIL from
Pseudomonas aeruginosa: Thermodynamics data correlated with
X-ray structures

J 2006

Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures

SABIN, Charles, Edward P. MITCHELL, Martina POKORNÁ, Catherine GAUTIER, J. UTILE et. al.

Basic information

Original name

Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures

Name in Czech

Vazba ruznych monosacharidu lektinem PA-IIL z Pseudomonas aeruginosa: korelace termodynamickych dat s X-ray strukturami

Authors

SABIN, Charles (250 France), Edward P. MITCHELL (826 United Kingdom of Great Britain and Northern Ireland), Martina POKORNÁ (203 Czech Republic), Catherine GAUTIER (250 France), J. UTILE (250 France), Michaela WIMMEROVÁ (203 Czech Republic, guarantor) and Anne IMBERTY (250 France)

Edition

FEBS Letters, Amsterdam, Elsevier Science B.V. 2006, 0014-5793

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.372

RIV identification code

RIV/00216224:14310/06:00016740

Organization unit

Faculty of Science

UT WoS

000235222500040

Keywords in English

Pseudomonas aeruginosa; lectin; cystic fibrosis

Abstract

ORIG CZ

V originále

The PA-IIL lectin from Pseudomonas aeruginosa is involved in host recognition and biofilm formation. The lectin displays an unusually high affinity for fucose but also binds to L-fucose, L-galactose and D-arabinose that differ only by the group at position 5 of the sugar ring. ITC experiments provided precise determination of affinity for the three methyl-glycosides and revealed a large enthalpy contribution. The crystal structures of the complexes of PA-IIL with L-galactose and Met-â-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. Combination of structures and thermodynamics provided clues for the role of the hydrophobic group in affinity.

In Czech

Vazba ruznych monosacharidu lektinem PA-IIL z Pseudomonas aeruginosa: korelace termodynamickych dat s X-ray strukturami

Links

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Citovat

SABIN, Charles, Edward P. MITCHELL, Martina POKORNÁ, Catherine GAUTIER, J. UTILE, Michaela WIMMEROVÁ and Anne IMBERTY. Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures. FEBS Letters. Amsterdam: Elsevier Science B.V., 2006, vol. 580, No 2, p. 982-987. ISSN 0014-5793.

@article{633505,
   author = {Sabin, Charles and Mitchell, Edward P. and Pokorná, Martina and Gautier, Catherine and Utile, J. and Wimmerová, Michaela and Imberty, Anne},
   article_location = {Amsterdam},
   article_number = {2},
   keywords = {Pseudomonas aeruginosa; lectin; cystic fibrosis},
   language = {eng},
   issn = {0014-5793},
   journal = {FEBS Letters},
   title = {Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures},
   volume = {580},
   year = {2006}
}

TY  - JOUR
ID  - 633505
AU  - Sabin, Charles - Mitchell, Edward P. - Pokorná, Martina - Gautier, Catherine - Utile, J. - Wimmerová, Michaela - Imberty, Anne
PY  - 2006
TI  - Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures
JF  - FEBS Letters
VL  - 580
IS  - 2
SP  - 982-987
EP  - 982-987
PB  - Elsevier Science B.V.
SN  - 00145793
KW  - Pseudomonas aeruginosa
KW  - lectin
KW  - cystic fibrosis
N2  - The PA-IIL lectin from Pseudomonas aeruginosa is involved in host recognition and biofilm formation. The lectin displays an unusually high affinity for fucose but also binds to L-fucose, L-galactose and D-arabinose that differ only by the group at position 5 of the sugar ring. ITC experiments provided precise determination of affinity for the three methyl-glycosides and revealed a large enthalpy contribution. The crystal structures of the complexes of PA-IIL with L-galactose and Met-â-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. Combination of structures and thermodynamics provided clues for the role of the hydrophobic group in affinity.
ER  -

SABIN, Charles, Edward P. MITCHELL, Martina POKORNÁ, Catherine GAUTIER, J. UTILE, Michaela WIMMEROVÁ and Anne IMBERTY. Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures. \textit{FEBS Letters}. Amsterdam: Elsevier Science B.V., 2006, vol.~580, No~2, p.~982-987. ISSN~0014-5793.

Detailed Information on Publication Record