4thi

From Proteopedia

(Difference between revisions)

Current revision

THIAMINASE I FROM BACILLUS THIAMINOLYTICUS WITH COVALENTLY BOUND 4-AMINO-2,5-DIMETHYLPYRIMIDINE

Structural highlights

4thi is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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.

References

↑ Campobasso N, Costello CA, Kinsland C, Begley TP, Ealick SE. Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 A resolution. Biochemistry. 1998 Nov 10;37(45):15981-9. PMID:9843405 doi:http://dx.doi.org/10.1021/bi981673l

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4thi"

Categories: Bacillus subtilis | Large Structures | Begley TP | Campobasso N | Ealick SE

@@ Line 1: / Line 1: @@
 ==THIAMINASE I FROM BACILLUS THIAMINOLYTICUS WITH COVALENTLY BOUND 4-AMINO-2,5-DIMETHYLPYRIMIDINE==
-<StructureSection load='4thi' size='340' side='right' caption='[[4thi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4thi' size='340' side='right'caption='[[4thi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4thi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4THI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4THI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4thi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4THI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4THI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYD:2,5-DIMETHYL-PYRIMIDIN-4-YLAMINE'>PYD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYD:2,5-DIMETHYL-PYRIMIDIN-4-YLAMINE'>PYD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4thi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4thi OCA], [http://pdbe.org/4thi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4thi RCSB], [http://www.ebi.ac.uk/pdbsum/4thi PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4thi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4thi OCA], [https://pdbe.org/4thi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4thi RCSB], [https://www.ebi.ac.uk/pdbsum/4thi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4thi ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/THI1_PANTH THI1_PANTH]] Degrades thiamine by replacing its thiazole moiety with a wide range of nucleophiles.
+[https://www.uniprot.org/uniprot/THI1_PANTH THI1_PANTH] Degrades thiamine by replacing its thiazole moiety with a wide range of nucleophiles.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/4thi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/4thi_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 4thi" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Thiaminase|Thiaminase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Bacillus subtilis]]
-[[Category: Thiamine pyridinylase]]
+[[Category: Large Structures]]
-[[Category: Begley, T P]]
+[[Category: Begley TP]]
-[[Category: Campobasso, N]]
+[[Category: Campobasso N]]
-[[Category: Ealick, S E]]
+[[Category: Ealick SE]]
-[[Category: Thiamin degradation]]
-[[Category: Transferase]]

4thi

From Proteopedia

Current revision

THIAMINASE I FROM BACILLUS THIAMINOLYTICUS WITH COVALENTLY BOUND 4-AMINO-2,5-DIMETHYLPYRIMIDINE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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