2thi: Difference between revisions

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[[Image:2thi.jpg|left|200px]]
[[Image:2thi.jpg|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiamine_pyridinylase Thiamine pyridinylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.2 2.5.1.2] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2thi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2thi OCA], [http://www.ebi.ac.uk/pdbsum/2thi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2thi RCSB]</span>
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'''THIAMINASE I FROM BACILLUS THIAMINOLYTICUS'''
'''THIAMINASE I FROM BACILLUS THIAMINOLYTICUS'''
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[[Category: Campobasso, N.]]
[[Category: Campobasso, N.]]
[[Category: Ealick, S E.]]
[[Category: Ealick, S E.]]
[[Category: thiamine degradation]]
[[Category: Thiamine degradation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:24:03 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:03:44 2008''

Revision as of 17:24, 4 May 2008

File:2thi.jpg

Template:STRUCTURE 2thi

THIAMINASE I FROM BACILLUS THIAMINOLYTICUS


OverviewOverview

Thiaminase-I catalyzes the replacement of the thiazole moiety of thiamin with a wide variety of nucleophiles, such as pyridine, aniline, catechols, quinoline, and cysteine. The crystal structure of the enzyme from Bacillus thiaminolyticus was determined at 2.5 A resolution by multiple isomorphous replacement and refined to an R factor of 0.195 (Rfree = 0.272). Two other structures, one native and one containing a covalently bound inhibitor, were determined at 2.0 A resolution by molecular replacement from a second crystal form and were refined to R factors of 0.205 and 0.217 (Rfree = 0.255 and 0.263), respectively. The overall structure contains two alpha/beta-type domains separated by a large cleft. At the base of the cleft lies Cys113, previously identified as a key active site nucleophile. The structure with a covalently bound thiamin analogue, which functions as a mechanism-based inactivating agent, confirms the location of the active site. Glu241 appears to function as an active site base to increase the nucleophilicity of Cys113. The mutant Glu241Gln was made and shows no activity. Thiaminase-I shows no sequence identity to other proteins in the sequence databases, but the three-dimensional structure shows very high structural homology to the periplasmic binding proteins and the transferrins.

About this StructureAbout this Structure

2THI is a Single protein structure of sequence from Paenibacillus thiaminolyticus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 A resolution., Campobasso N, Costello CA, Kinsland C, Begley TP, Ealick SE, Biochemistry. 1998 Nov 10;37(45):15981-9. PMID:9843405 Page seeded by OCA on Sun May 4 17:24:03 2008

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