1g4e: Difference between revisions

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-[[Image:1g4e.jpg|left|200px]]
- {{Structure
+==THIAMIN PHOSPHATE SYNTHASE==
-|PDB= 1g4e |SIZE=350|CAPTION= <scene name='initialview01'>1g4e</scene>, resolution 1.60&Aring;
+<StructureSection load='1g4e' size='340' side='right'caption='[[1g4e]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1g4e]] is a 2 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=1G4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G4E FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Thiamine-phosphate_diphosphorylase Thiamine-phosphate diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.3 2.5.1.3]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-|GENE= THIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4e OCA], [https://pdbe.org/1g4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g4e RCSB], [https://www.ebi.ac.uk/pdbsum/1g4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g4e ProSAT]</span></td></tr>
-}}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/THIE_BACSU THIE_BACSU] Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP.<ref>PMID:9139923</ref> <ref>PMID:11513588</ref>
+== 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/g4/1g4e_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g4e ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thiamin phosphate synthase catalyzes the formation of thiamin phosphate from 4-amino-5-(hydroxymethyl)-2-methylpyrimidine pyrophosphate and 5-(hydroxyethyl)-4-methylthiazole phosphate. Several lines of evidence suggest that the reaction proceeds via a dissociative mechanism. The previously determined crystal structure of thiamin phosphate synthase in complex with the reaction products, thiamin phosphate and magnesium pyrophosphate, provided a view of the active site and suggested a number of additional experiments. We report here seven new crystal structures primarily involving crystals of S130A thiamin phosphate synthase soaked in solutions containing substrates or products. We prepared S130A thiamin phosphate synthase with the intent of characterizing the enzyme-substrate complex. Surprisingly, in three thiamin phosphate synthase structures, the active site density cannot be modeled as either substrates or products. For these structures, the best fit to the electron density is provided by a model that consists of independent pyrimidine, pyrophosphate, and thiazole phosphate fragments, consistent with a carbenium ion intermediate. The resulting carbenium ion is likely to be further stabilized by proton transfer from the pyrimidine amino group to the pyrophosphate to give the pyrimidine iminemethide, which we believe is the species that is observed in the crystal structures.
-'''THIAMIN PHOSPHATE SYNTHASE'''
+Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase.,Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:11513589<ref>PMID:11513589</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1g4e" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Thiamin phosphate synthase catalyzes the formation of thiamin phosphate from 4-amino-5-(hydroxymethyl)-2-methylpyrimidine pyrophosphate and 5-(hydroxyethyl)-4-methylthiazole phosphate. Several lines of evidence suggest that the reaction proceeds via a dissociative mechanism. The previously determined crystal structure of thiamin phosphate synthase in complex with the reaction products, thiamin phosphate and magnesium pyrophosphate, provided a view of the active site and suggested a number of additional experiments. We report here seven new crystal structures primarily involving crystals of S130A thiamin phosphate synthase soaked in solutions containing substrates or products. We prepared S130A thiamin phosphate synthase with the intent of characterizing the enzyme-substrate complex. Surprisingly, in three thiamin phosphate synthase structures, the active site density cannot be modeled as either substrates or products. For these structures, the best fit to the electron density is provided by a model that consists of independent pyrimidine, pyrophosphate, and thiazole phosphate fragments, consistent with a carbenium ion intermediate. The resulting carbenium ion is likely to be further stabilized by proton transfer from the pyrimidine amino group to the pyrophosphate to give the pyrimidine iminemethide, which we believe is the species that is observed in the crystal structures.
+*[[Thiamin phosphate synthase|Thiamin phosphate synthase]]
+== References ==
-==About this Structure==
+<references/>
-G4E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4E OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase., Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE, Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11513589 11513589]
 [[Category: Bacillus subtilis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Thiamine-phosphate diphosphorylase]]
+[[Category: Begley TP]]
-[[Category: Begley, T P.]]
+[[Category: Campobasso N]]
-[[Category: Campobasso, N.]]
+[[Category: Chiu H-J]]
-[[Category: Chiu, H J.]]
+[[Category: Ealick SE]]
-[[Category: Ealick, S E.]]
+[[Category: Peapus DH]]
-[[Category: Peapus, D H.]]
+[[Category: Reddick JJ]]
-[[Category: Reddick, J J.]]
-[[Category: thiamin biosynthesis]]
-[[Category: tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:04 2008''