1uzv: Difference between revisions

Revision as of 01:04, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1uzv.png

Template:STRUCTURE 1uzv

HIGH AFFINITY FUCOSE BINDING OF PSEUDOMONAS AERUGINOSA LECTIN II: 1.0 A CRYSTAL STRUCTURE OF THE COMPLEXHIGH AFFINITY FUCOSE BINDING OF PSEUDOMONAS AERUGINOSA LECTIN II: 1.0 A CRYSTAL STRUCTURE OF THE COMPLEX

Template:ABSTRACT PUBMED 15573375

About this StructureAbout this Structure

1UZV is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

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., Mitchell EP, Sabin C, Snajdrova L, Pokorna M, Perret S, Gautier C, Hofr C, Gilboa-Garber N, Koca J, Wimmerova M, Imberty A, Proteins. 2005 Feb 15;58(3):735-46. PMID:15573375

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''HIGH AFFINITY FUCOSE BINDING OF PSEUDOMONAS AERUGINOSA LECTIN II: 1.0 A CRYSTAL STRUCTURE OF THE COMPLEX'''
+===HIGH AFFINITY FUCOSE BINDING OF PSEUDOMONAS AERUGINOSA LECTIN II: 1.0 A CRYSTAL STRUCTURE OF THE COMPLEX===
-==Overview==
+<!--
-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.
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 ==About this Structure==
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 [[Category: Fucose]]
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