1sqj
From Proteopedia
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Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)
Overview
Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.
About this Structure
1SQJ is a Single protein structure of sequence from Geotrichum sp. m128. Active as Oligoxyloglucan reducing-end-specific cellobiohydrolase, with EC number 3.2.1.150 Full crystallographic information is available from OCA.
Reference
Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase., Yaoi K, Kondo H, Noro N, Suzuki M, Tsuda S, Mitsuishi Y, Structure. 2004 Jul;12(7):1209-17. PMID:15242597
Page seeded by OCA on Thu Feb 21 15:04:10 2008
