1fhl
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(New page: 200px<br /><applet load="1fhl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fhl, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 12:48, 20 November 2007
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CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K
Overview
The three-dimensional structure of Aspergillus aculeatus, beta-1,4-galactanase (AAGAL), an enzyme involved in pectin degradation, has been determined by multiple isomorphous replacement to 2.3 and 1.8 A, resolution at 293 and 100 K, respectively. It represents the first known, structure for a polysaccharidase with this specificity and for a member of, glycoside hydrolase family 53 (GH-53). The enzyme folds into a, (beta/alpha)(8) barrel with the active site cleft located at the, C-terminal side of the barrel consistent with the classification of GH-53, in clan GH-A, a superfamily of enzymes with common fold and catalytic, machinery but diverse specificities. Putative substrate-enzyme, interactions were elucidated by modeling of beta-1,4-linked galactobioses, into the possible substrate binding subsites. The structure and modeling, studies identified five potential subsites for the binding of galactans, of which one is a pocket suited for accommodating the arabinan side chain, in arabinogalactan, one of the natural substrates. A comparison with the, substrate binding grooves of other Clan GH-A enzymes suggests that shape, complementarity is crucial in determining the specificity of, polysaccharidases.
About this Structure
1FHL is a Single protein structure of sequence from Aspergillus aculeatus. Active as Arabinogalactan endo-1,4-beta-galactosidase, with EC number 3.2.1.89 Full crystallographic information is available from OCA.
Reference
Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A., Ryttersgaard C, Lo Leggio L, Coutinho PM, Henrissat B, Larsen S, Biochemistry. 2002 Dec 24;41(51):15135-43. PMID:12484750
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