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1bs9
From Proteopedia
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ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS
Overview
Enzymatic and non-enzymatic iodination of the amino acid tyrosine is a, well known phenomenon. The iodination technique has been widely used for, labeling proteins. Using high-resolution X-ray crystallographic, techniques, the chemical and three-dimensional structures of iodotyrosines, formed by non-enzymatic incorporation of I atoms into tyrosine residues of, a crystalline protein are described. Acetylxylan esterase (AXE II; 207, amino-acid residues) from Penicillium purpurogenum has substrate, specificities towards acetate esters of D-xylopyranose residues in xylan, and belongs to a new class of alpha/beta hydrolases. The crystals of the, enzyme are highly ordered, tightly packed and diffract to better than, sub-angstrom resolution at 85 K. The iodination technique has been, utilized to ... [(full description)]
About this Structure
1BS9 is a [Single protein] structure of sequence from [Penicillium purpurogenum] with SO4 as [ligand]. Active as [[1]], with EC number [3.1.1.6]. Full crystallographic information is available from [OCA].
Reference
Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase., Ghosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jornvall H, Gutierrez R, Eyzaguirre J, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):779-84. PMID:10089308
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