3wdm
From Proteopedia
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| - | + | ==Crystal structure of 4-phosphopantoate-beta-alanine ligase from Thermococcus kodakarensis== | |
| - | + | <StructureSection load='3wdm' size='340' side='right' caption='[[3wdm]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3wdm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WDM FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wdk|3wdk]], [[3wdl|3wdl]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK1686 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-phosphopantoate--beta-alanine_ligase 4-phosphopantoate--beta-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.36 6.3.2.36] </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=3wdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wdm RCSB], [http://www.ebi.ac.uk/pdbsum/3wdm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/PPS_THEKO PPS_THEKO]] Catalyzes the conversion of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. Cannot use (R)-pantoate as substrate and thus does not display pantothenate synthetase (PS) activity. | [[http://www.uniprot.org/uniprot/PPS_THEKO PPS_THEKO]] Catalyzes the conversion of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. Cannot use (R)-pantoate as substrate and thus does not display pantothenate synthetase (PS) activity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria/eukaryotes share a common pathway for coenzyme A biosynthesis which involves two enzymes to convert pantoate to 4'-phosphopantothenate. These two enzymes are absent in almost all archaea. Recently, it was reported that two novel enzymes, pantoate kinase (PoK) and phosphopantothenate synthetase (PPS), are responsible for this conversion in archaea. Here, we report the crystal structure of PPS from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complexes with substrates, ATP, and ATP and 4-phosphopantoate (PPo). PPS forms an asymmetric homodimer, in which two monomers composing a dimer, deviated from the exact 2-fold symmetry, displaying 4 degrees -13 degrees distortion. The structural features are consistent with the mutagenesis data and the results of biochemical experiments previously reported. Based on these structures, we discuss the catalytic mechanism by which PPS produces phosphopantoyl adenylate (PPA), which is thought to be a reaction intermediate. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc. | ||
| - | + | Crystal Structure of Phosphopantothenate Synthetase from Thermococcus k odakarensis.,Kishimoto A, Kita A, Ishibashi T, Tomita H, Yokooji Y, Imanaka T, Atomi H, Miki K Proteins. 2014 Mar 17. doi: 10.1002/prot.24546. PMID:24638914<ref>PMID:24638914</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: 4-phosphopantoate--beta-alanine ligase]] | [[Category: 4-phosphopantoate--beta-alanine ligase]] | ||
| - | [[Category: Atomi, H | + | [[Category: Atomi, H]] |
| - | [[Category: Imanaka, T | + | [[Category: Imanaka, T]] |
| - | [[Category: Ishibashi, T | + | [[Category: Ishibashi, T]] |
| - | [[Category: Kishimoto, A | + | [[Category: Kishimoto, A]] |
| - | [[Category: Kita, A | + | [[Category: Kita, A]] |
| - | [[Category: Miki, K | + | [[Category: Miki, K]] |
| - | [[Category: Tomita, H | + | [[Category: Tomita, H]] |
| - | [[Category: Yokooji, Y | + | [[Category: Yokooji, Y]] |
[[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 07:21, 24 December 2014
Crystal structure of 4-phosphopantoate-beta-alanine ligase from Thermococcus kodakarensis
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