1bs9: Difference between revisions

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[[Image:1bs9.jpg|left|200px]]
[[Image:1bs9.jpg|left|200px]]


{{Structure
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|PDB= 1bs9 |SIZE=350|CAPTION= <scene name='initialview01'>1bs9</scene>, resolution 1.10&Aring;
The line below this paragraph, containing "STRUCTURE_1bs9", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=CAT:These+Three+Residues+Form+The+Catalytic+Triad'>CAT</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
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|DOMAIN=
{{STRUCTURE_1bs9| PDB=1bs9  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bs9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bs9 OCA], [http://www.ebi.ac.uk/pdbsum/1bs9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bs9 RCSB]</span>
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'''ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS'''
'''ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT 1.10 ANGSTROMS'''
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[[Category: Thiel, D J.]]
[[Category: Thiel, D J.]]
[[Category: Weeks, D R.]]
[[Category: Weeks, D R.]]
[[Category: alpha/beta hydrolase]]
[[Category: Alpha/beta hydrolase]]
[[Category: esterase]]
[[Category: Esterase]]
[[Category: serine hydrolase]]
[[Category: Serine hydrolase]]
 
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Revision as of 11:53, 2 May 2008

File:1bs9.jpg

Template:STRUCTURE 1bs9

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 Page seeded by OCA on Fri May 2 11:53:51 2008

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