1fhl
From Proteopedia
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'''CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K''' | '''CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K''' | ||
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[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
[[Category: Ryttersgaard, C.]] | [[Category: Ryttersgaard, C.]] | ||
| - | [[Category: | + | [[Category: B/a barrel]] |
| - | [[Category: | + | [[Category: Clan gh-a]] |
| - | [[Category: | + | [[Category: Family 53]] |
| - | [[Category: | + | [[Category: Glycosyl hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:20:02 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:20, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 16:20:02 2008
