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1bs9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Enzymatic and non-enzymatic iodination of the amino acid tyrosine is a | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Li, N.]] | [[Category: Li, N.]] | ||
[[Category: Pangborn, W.]] | [[Category: Pangborn, W.]] | ||
| - | [[Category: Sawicki, M | + | [[Category: Sawicki, M W.]] |
| - | [[Category: Thiel, D | + | [[Category: Thiel, D J.]] |
| - | [[Category: Weeks, D | + | [[Category: Weeks, D R.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alpha/beta hydrolase]] | [[Category: alpha/beta hydrolase]] | ||
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[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:36 2008'' |
Revision as of 09:58, 21 February 2008
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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 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.
About this Structure
1BS9 is a Single protein structure of sequence from Penicillium purpurogenum with as ligand. Active as Acetylesterase, with EC number 3.1.1.6 Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 11:58:36 2008
