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| - | [[Image:1ks9.jpg|left|200px]] | |
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| - | {{Structure
| + | ==Ketopantoate Reductase from Escherichia coli== |
| - | |PDB= 1ks9 |SIZE=350|CAPTION= <scene name='initialview01'>1ks9</scene>, resolution 1.70Å
| + | <StructureSection load='1ks9' size='340' side='right'caption='[[1ks9]], [[Resolution|resolution]] 1.70Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1ks9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KS9 FirstGlance]. <br> |
| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/2-dehydropantoate_2-reductase 2-dehydropantoate 2-reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.169 1.1.1.169] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | |GENE= panE (apbA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ks9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ks9 OCA], [https://pdbe.org/1ks9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ks9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ks9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ks9 ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY=
| + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ks9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ks9 OCA], [http://www.ebi.ac.uk/pdbsum/1ks9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ks9 RCSB]</span>
| + | [https://www.uniprot.org/uniprot/PANE_ECOLI PANE_ECOLI] Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. |
| - | }}
| + | == Evolutionary Conservation == |
| - | | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | '''Ketopantoate Reductase from Escherichia coli'''
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/1ks9_consurf.spt"</scriptWhenChecked> |
| - | ==Overview== | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | Ketopantoate reductase (KPR, EC 1.1.1.169) catalyzes the NADPH-dependent reduction of ketopantoate to pantoate on the pantothenate (vitamin B(5)) biosynthetic pathway. The Escherichia coli panE gene encoding KPR was cloned and expressed at high levels as the native and selenomethionine-substituted (SeMet) proteins. Both native and SeMet recombinant proteins were purified by three chromatographic steps, to yield pure proteins. The wild-type enzyme was found to have a K(M)(NADPH) of 20 microM, a K(M)(ketopantoate) of 60 microM, and a k(cat) of 40 s(-1). Regular prismatic KPR crystals were prepared using the hanging drop technique. They belonged to the tetragonal space group P4(2)2(1)2, with cell parameters: a = b = 103.7 A and c = 55.7 A, accommodating one enzyme molecule per asymmetric unit. The structure of KPR was determined by the multiwavelength anomalous dispersion method using the SeMet protein, for which data were collected to 2.3 A resolution. The native data were collected to 1.7 A resolution and used to refine the final structure. The secondary structure comprises 12 alpha-helices, three 3(10)-helices, and 11 beta-strands. The enzyme is monomeric and has two domains separated by a cleft. The N-terminal domain has an alphabeta-fold of the Rossmann type. The C-terminal domain (residues 170-291) is composed of eight alpha-helices. KPR is shown to be a member of the 6-phosphogluconate dehydrogenase C-terminal domain-like superfamily. A model for the ternary enzyme-NADPH-ketopantoate ternary complex provides a rationale for kinetic data reported for specific site-directed mutants.
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ==About this Structure==
| + | </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=1ks9 ConSurf]. |
| - | 1KS9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KS9 OCA].
| + | <div style="clear:both"></div> |
| - | | + | __TOC__ |
| - | ==Reference== | + | </StructureSection> |
| - | Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism., Matak-Vinkovic D, Vinkovic M, Saldanha SA, Ashurst JL, von Delft F, Inoue T, Miguel RN, Smith AG, Blundell TL, Abell C, Biochemistry. 2001 Dec 4;40(48):14493-500. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11724562 11724562]
| + | |
| - | [[Category: 2-dehydropantoate 2-reductase]]
| + | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Abell, C.]] | + | [[Category: Abell C]] |
| - | [[Category: Ashurst, J A.]] | + | [[Category: Ashurst JA]] |
| - | [[Category: Blundell, T L.]] | + | [[Category: Blundell TL]] |
| - | [[Category: Delft, F von.]]
| + | [[Category: Inoue T]] |
| - | [[Category: Inoue, T.]] | + | [[Category: Matak-Vinkovic D]] |
| - | [[Category: Matak-Vinkovic, D.]] | + | [[Category: Miguel RN]] |
| - | [[Category: Miguel, R N.]] | + | [[Category: Saldanha SA]] |
| - | [[Category: Saldanha, S A.]] | + | [[Category: Smith AG]] |
| - | [[Category: Smith, A G.]] | + | [[Category: Vinkovic M]] |
| - | [[Category: Vinkovic, M.]] | + | [[Category: Von Delft F]] |
| - | [[Category: apba]] | + | |
| - | [[Category: apo]]
| + | |
| - | [[Category: ketopantoate reductase]]
| + | |
| - | [[Category: monomer]]
| + | |
| - | [[Category: pane]]
| + | |
| - | [[Category: rossman fold]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:50 2008''
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