1us2
From Proteopedia
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XYLANASE10C (MUTANT E385A) FROM CELLVIBRIO JAPONICUS IN COMPLEX WITH XYLOPENTAOSE
Overview
Microbial degradation of the plant cell wall is the primary mechanism by, which carbon is utilized in the biosphere. The hydrolysis of xylan, by, endo-beta-1,4-xylanases (xylanases), is one of the key reactions in this, process. Although amino acid sequence variations are evident in the, substrate binding cleft of "family GH10" xylanases (see, afmb.cnrs-mrs.fr/CAZY/), their biochemical significance is unclear. The, Cellvibrio japonicus GH10 xylanase CjXyn10C is a bi-modular enzyme, comprising a GH10 catalytic module and a family 15 carbohydrate-binding, module. The three-dimensional structure at 1.85 A, presented here, shows, that the sequence joining the two modules is disordered, confirming that, linker sequences in modular glycoside hydrolases are highly flexible., CjXyn10C hydrolyzes ... [(full description)]
About this Structure
1US2 is a [Single protein] structure of sequence from [Cellvibrio japonicus]. Active as [[1]], with EC number [3.2.1.8]. Full crystallographic information is available from [OCA].
Reference
Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases., Pell G, Szabo L, Charnock SJ, Xie H, Gloster TM, Davies GJ, Gilbert HJ, J Biol Chem. 2004 Mar 19;279(12):11777-88. Epub 2003 Dec 11. PMID:14670951
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