1bvv: Difference between revisions
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Revision as of 15:53, 30 October 2007
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SUGAR RING DISTORTION IN THE GLYCOSYL-ENZYME INTERMEDIATE OF A FAMILY G/11 XYLANASE
OverviewOverview
The 1.8 A resolution structure of the glycosyl-enzyme intermediate formed, on the retaining beta-1,4-xylanase from Bacillus circulans has been, determined using X-ray crystallographic techniques. The 2-fluoro-xylose, residue bound in the -1 subsite adopts a 2,5B (boat) conformation, allowing atoms C5, O5, C1, and C2 of the sugar to achieve coplanarity as, required at the oxocarbenium ion-like transition states of the, double-displacement catalytic mechanism. Comparison of this structure to, that of a mutant of this same enzyme noncovalently complexed with, xylotetraose [Wakarchuk et al. (1994) Protein Sci. 3, 467-475] reveals a, number of differences beyond the distortion of the sugar moiety. Most, notably, a bifurcated hydrogen bond interaction is formed in the, glycosyl-enzyme ... [(full description)]
About this StructureAbout this Structure
1BVV is a [Single protein] structure of sequence from [Bacillus circulans] with XYP and DFX as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Sites: ABC and NUC. Full crystallographic information is available from [OCA].
ReferenceReference
Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase., Sidhu G, Withers SG, Nguyen NT, McIntosh LP, Ziser L, Brayer GD, Biochemistry. 1999 Apr 27;38(17):5346-54. PMID:10220321
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