1UZV

High affinity fucose binding of Pseudomonas aeruginosa lectin II: 1.0 A crystal structure of the complex

Summary for 1UZV

• Entry DOI: 10.2210/pdb1uzv/pdb
• Related: 1GZT 1OUR 1OUS 1OUX 1OVP 1OVS 1OXC 1W38 1W43 1W8F 1W8H
• Descriptor: PSEUDOMONAS AERUGINOSA LECTIN II, SULFATE ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: lectin, fucose, calcium
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 4
• Total formula weight: 48108.20

Authors

Mitchell, E.,Sabin, C.D.,Snajdrova, L.,Budova, M.,Perret, S.,Gautier, C.,Gilboa-Garber, N.,Koca, J.,Wimmerova, M.,Imberty, A. (deposition date: 2004-03-17, release date: 2004-12-08, Last modification date: 2024-05-01)

Primary citation

Mitchell, E.P.,Sabin, C.,Snajdrova, L.,Pokorna, M.,Perret, S.,Gautier, C.,Hofr, C.,Gilboa-Garber, N.,Koca, J.,Wimmerova, M.,Imberty, A.
High Affinity Fucose Binding of Pseudomonas Aeruginosa Lectin Pa-Iil: 1.0 A Resolution Crystal Structure of the Complex Combined with Thermodynamics and Computational Chemistry Approaches.
Proteins, 58:735-, 2005

PubMed Abstract: PA-IIL is a fucose-binding lectin from Pseudomonas aeruginosa that is closely related to the virulence factors of the bacterium. Previous structural studies have revealed a new carbohydrate-binding mode with direct involvement of two calcium ions (Mitchell E, Houles C, Sudakevitz D, Wimmerova M, Gautier C, Perez S, Wu AM, Gilboa-Garber N, Imberty A. Structural basis for selective recognition of oligosaccharides from cystic fibrosis patients by the lectin PA-IIL of Pseudomonas aeruginosa. Nat Struct Biol 2002;9:918-921). A combination of thermodynamic, structural, and computational methods has been used to study the basis of the high affinity for the monosaccharide ligand. A titration microcalorimetry study indicated that the high affinity is enthalpy driven. The crystal structure of the tetrameric PA-IIL in complex with fucose and calcium was refined to 1.0 A resolution and, in combination with modeling, allowed a proposal to be made for the hydrogen-bond network in the binding site. Calculations of partial charges using ab initio computational chemistry methods indicated that extensive delocalization of charges between the calcium ions, the side chains of the protein-binding site and the carbohydrate ligand is responsible for the high enthalpy of binding and therefore for the unusually high affinity observed for this unique mode of carbohydrate recognition.

PubMed: 15573375
DOI: 10.1002/PROT.20330

Experimental method

X-RAY DIFFRACTION (1 Å)