2ead: Difference between revisions

Revision as of 15:34, 29 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:2ead.png

Template:STRUCTURE 2ead

Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with substrateCrystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with substrate

Template:ABSTRACT PUBMED 17459873

About this StructureAbout this Structure

2EAD is a Single protein structure of sequence from Bifidobacterium bifidum. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum., Nagae M, Tsuchiya A, Katayama T, Yamamoto K, Wakatsuki S, Kato R, J Biol Chem. 2007 Jun 22;282(25):18497-509. Epub 2007 Apr 25. PMID:17459873

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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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-[[Image:2ead.gif|left|200px]]
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 {{STRUCTURE_2ead|  PDB=2ead  |  SCENE=  }}
-'''Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with substrate'''
+===Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with substrate===
-==Overview==
+<!--
-,2-alpha-L-fucosidase (AfcA), which hydrolyzes the glycosidic linkage of Fucalpha1-2Gal via an inverting mechanism, was recently isolated from Bifidobacterium bifidum and classified as the first member of the novel glycoside hydrolase family 95. To better understand the molecular mechanism of this enzyme, we determined the x-ray crystal structures of the AfcA catalytic (Fuc) domain in unliganded and complexed forms with deoxyfuconojirimycin (inhibitor), 2'-fucosyllactose (substrate), and L-fucose and lactose (products) at 1.12-2.10 A resolution. The AfcA Fuc domain is composed of four regions, an N-terminal beta region, a helical linker, an (alpha/alpha)6 helical barrel domain, and a C-terminal beta region, and this arrangement is similar to bacterial phosphorylases. In the complex structures, the ligands were buried in the central cavity of the helical barrel domain. Structural analyses in combination with mutational experiments revealed that the highly conserved Glu566 probably acts as a general acid catalyst. However, no carboxylic acid residue is found at the appropriate position for a general base catalyst. Instead, a water molecule stabilized by Asn423 in the substrate-bound complex is suitably located to perform a nucleophilic attack on the C1 atom of L-fucose moiety in 2'-fucosyllactose, and its location is nearly identical near the O1 atom of beta-L-fucose in the products-bound complex. Based on these data, we propose and discuss a novel catalytic reaction mechanism of AfcA.
+The line below this paragraph, {{ABSTRACT_PUBMED_17459873}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17459873 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17459873}}
 ==About this Structure==
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 [[Category: Fucosidase]]
 [[Category: Glycoside hydrolase]]
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