2thi: Difference between revisions
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<StructureSection load='2thi' size='340' side='right'caption='[[2thi]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2thi' size='340' side='right'caption='[[2thi]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2thi]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2thi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_thiaminolyticus"_kuno_1951 "bacillus thiaminolyticus" kuno 1951]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2THI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2THI FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiamine_pyridinylase Thiamine pyridinylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.2 2.5.1.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2thi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2thi OCA], [https://pdbe.org/2thi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2thi RCSB], [https://www.ebi.ac.uk/pdbsum/2thi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2thi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/THI1_PANTH THI1_PANTH]] Degrades thiamine by replacing its thiazole moiety with a wide range of nucleophiles. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 15:28, 23 March 2022
THIAMINASE I FROM BACILLUS THIAMINOLYTICUSTHIAMINASE I FROM BACILLUS THIAMINOLYTICUS
Structural highlights
Function[THI1_PANTH] Degrades thiamine by replacing its thiazole moiety with a wide range of nucleophiles. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThiaminase-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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