1bs9: Difference between revisions
No edit summary |
No edit summary |
||
| Line 30: | Line 30: | ||
[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:57:05 2007'' | ||
Revision as of 15:52, 30 October 2007
|
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 ... [(full description)]
About this StructureAbout this Structure
1BS9 is a [Single protein] structure of sequence from [Penicillium purpurogenum] with SO4 as [ligand]. Active as [Acetylesterase], with EC number [3.1.1.6]. Structure known Active Site: CAT. 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 Tue Oct 30 14:57:05 2007