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| {{STRUCTURE_2axe| PDB=2axe | SCENE= }} | | {{STRUCTURE_2axe| PDB=2axe | SCENE= }} |
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| '''IODINATED COMPLEX OF ACETYL XYLAN ESTERASE AT 1.80 ANGSTROMS'''
| | ===IODINATED COMPLEX OF ACETYL XYLAN ESTERASE AT 1.80 ANGSTROMS=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10089308}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10089308 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10089308}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Iodotyrosine]] | | [[Category: Iodotyrosine]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:35:26 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:30:17 2008'' |
