2axe

IODINATED COMPLEX OF ACETYL XYLAN ESTERASE AT 1.80 ANGSTROMS

spinqualitylabelsall models 2axe, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2axe is a 1 chain structure with sequence from Penicillium purpurogenum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: TYI Activity: Acetylesterase, with EC number 3.1.1.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AXE2_PENPU] Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 prepare an isomorphous derivative of the AXE II crystal. The structure of the enzyme determined at 1.10 A resolution exclusively by normal and anomalous scattering from I atoms, along with the structure of the iodinated complex at 1.80 A resolution, demonstrate the formation of covalent bonds between I atoms and C atoms at ortho positions to the hydroxyl groups of two tyrosyl moieties, yielding iodotyrosines. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetylxylan esterase 3D structures

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