1bs9: Difference between revisions
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[[Image:1bs9.jpg|left|200px]] | [[Image:1bs9.jpg|left|200px]] | ||
'''ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS''' | {{Structure | ||
|PDB= 1bs9 |SIZE=350|CAPTION= <scene name='initialview01'>1bs9</scene>, resolution 1.10Å | |||
|SITE= <scene name='pdbsite=CAT:These+Three+Residues+Form+The+Catalytic+Triad'>CAT</scene> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</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] | |||
|GENE= | |||
}} | |||
'''ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BS9 is a [ | 1BS9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_purpurogenum Penicillium purpurogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BS9 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10089308 10089308] | ||
[[Category: Acetylesterase]] | [[Category: Acetylesterase]] | ||
[[Category: Penicillium purpurogenum]] | [[Category: Penicillium purpurogenum]] | ||
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[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:15:07 2008'' | ||
Revision as of 11:15, 20 March 2008
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| , resolution 1.10Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Acetylesterase, with EC number 3.1.1.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS
OverviewOverview
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 StructureAbout this Structure
1BS9 is a Single protein structure of sequence from Penicillium purpurogenum. Full crystallographic information is available from OCA.
ReferenceReference
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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