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1m3u

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Revision as of 14:17, 12 October 2017

Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate

Structural highlights

1m3u is a 10 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	PANB ("Bacillus coli" Migula 1895)
Activity:	3-methyl-2-oxobutanoate hydroxymethyltransferase, with EC number 2.1.2.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PANB_ECOLI] Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.^[1]

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

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Teller JH, Powers SG, Snell EE. Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. J Biol Chem. 1976 Jun 25;251(12):3780-5. PMID:776976
↑ von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C. Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites. Structure. 2003 Aug;11(8):985-96. PMID:12906829

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m3u"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate==
 <StructureSection load='1m3u' size='340' side='right' caption='[[1m3u]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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://oca.weizmann.ac.il/oca-docs/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]</span></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=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>
 </table>
 == Function ==

1m3u

From Proteopedia

Revision as of 14:17, 12 October 2017

Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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