1m3u

<table><tr><td colspan='2'>[[1m3u]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1M3U FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KPL:KETOPANTOATE'>KPL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PANB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.11 2.1.2.11] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m3u OCA], [http://pdbe.org/1m3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m3u RCSB], [http://www.ebi.ac.uk/pdbsum/1m3u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m3u ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PANB_ECOLI PANB_ECOLI]] Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.<ref>PMID:776976</ref>

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== Publication Abstract from PubMed ==

We report the crystal structure of E. coli ketopantoate hydroxymethyltransferase (KPHMT) at 1.9 A resolution, in complex with its product, ketopantoate. KPHMT catalyzes the first step in the biosynthesis of pantothenate (vitamin B(5)), the precursor of coenzyme A and the acyl carrier protein cofactor. The structure of the decameric enzyme was solved by multiwavelength anomalous dispersion to locate 160 selenomethionine sites and phase 560 kDa of protein, making it the largest structure solved by this approach. KPHMT adopts the (betaalpha)(8) barrel fold and is a member of the phosphoenolpyruvate/pyruvate superfamily. The active site contains a ketopantoate bidentately coordinated to Mg(2+). Similar binding is likely for the substrate, alpha-ketoisovalerate, orienting the C3 for deprotonation.

Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites.,von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C Structure. 2003 Aug;11(8):985-96. PMID:12906829<ref>PMID:12906829</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m3u" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: 3-methyl-2-oxobutanoate hydroxymethyltransferase]]

[[Category: Abell, C]]

[[Category: Blundell, T L]]

[[Category: Delft, F von]]

[[Category: Dhanaraj, V]]

[[Category: Inoue, T]]

[[Category: Ottenhof, H H]]

[[Category: Saldanha, S A]]

[[Category: Smith, A G]]

[[Category: Witty, M]]

[[Category: Beta-alpha-barrel]]

[[Category: Transferase]]