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2BOJ

crystal Structure of pseudomonas aeruginosa lectin (PA-IIL) complexed with methyl-B-D-Arabinopyranoside

Summary for 2BOJ
Entry DOI10.2210/pdb2boj/pdb
Related1GZT 1OUR 1OUS 1OUX 1OVP 1OVS 1OXC 1UZV 1W43 1W8F 1W8H 2BP6
DescriptorPSEUDOMONAS AERUGINOSA LECTIN II, methyl beta-D-arabinopyranoside, CALCIUM ION, ... (5 entities in total)
Functional Keywordslectin, arabinose, calcium, lewis a, cystic fibrosis
Biological sourcePSEUDOMONAS AERUGINOSA
Total number of polymer chains4
Total formula weight48012.14
Authors
Sabin, C.D.,Mitchell, E.P.,Wimmerova, M.,Imberty, A. (deposition date: 2005-04-12, release date: 2006-02-22, Last modification date: 2023-12-13)
Primary citationSabin, C.D.,Mitchell, E.P.,Pokarna, M.,Gautier, C.,Utille, J.-P.,Wimmerova, M.,Imberty, A.
Binding of Different Monosaccharides by Lectin Pa-Iil from Pseudoman Aeruginosa: Thermodynamics Data Correlated with X-Ray Structures.
FEBS Lett., 580:982-, 2006
Cited by
PubMed Abstract: The lectin from Pseudomonas aeruginosa (PA-IIL) is involved in host recognition and biofilm formation. Lectin not only 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. Isothermal calorimetry 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-beta-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. A combination of the structures and thermodynamics provided clues for the role of the hydrophobic group in affinity.
PubMed: 16438968
DOI: 10.1016/J.FEBSLET.2006.01.030
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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数据于2025-06-25公开中

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