2axe: Difference between revisions
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|PDB= 2axe |SIZE=350|CAPTION= <scene name='initialview01'>2axe</scene>, resolution 1.80Å | |PDB= 2axe |SIZE=350|CAPTION= <scene name='initialview01'>2axe</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Acetylesterase Acetylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.6 3.1.1.6] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylesterase Acetylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.6 3.1.1.6] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2axe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axe OCA], [http://www.ebi.ac.uk/pdbsum/2axe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2axe RCSB]</span> | |||
}} | }} | ||
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[[Category: Thiel, D J.]] | [[Category: Thiel, D J.]] | ||
[[Category: Weeks, D R.]] | [[Category: Weeks, D R.]] | ||
[[Category: esterase]] | [[Category: esterase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: iodotyrosine]] | [[Category: iodotyrosine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:58:34 2008'' | ||
Revision as of 22:58, 30 March 2008
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| 2axe, resolution 1.80Å | |||||||||||||
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| Ligands: | SO4, TYI | ||||||||||||
| Activity: | Acetylesterase, with EC number 3.1.1.6 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
IODINATED COMPLEX OF ACETYL XYLAN ESTERASE AT 1.80 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
2AXE is a Single protein structure of sequence from Penicillium purpurogenum. 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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