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| | <StructureSection load='1yjq' size='340' side='right'caption='[[1yjq]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='1yjq' size='340' side='right'caption='[[1yjq]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yjq]] is a 1 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=1YJQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YJQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yjq]] 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=1YJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ks9|1ks9]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">panE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjq OCA], [https://pdbe.org/1yjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yjq RCSB], [https://www.ebi.ac.uk/pdbsum/1yjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjq ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjq OCA], [http://pdbe.org/1yjq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yjq RCSB], [http://www.ebi.ac.uk/pdbsum/1yjq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PANE_ECOLI PANE_ECOLI]] Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. | + | [https://www.uniprot.org/uniprot/PANE_ECOLI PANE_ECOLI] Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: 2-dehydropantoate 2-reductase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abell, C]] | + | [[Category: Abell C]] |
| - | [[Category: Blundell, T L]] | + | [[Category: Blundell TL]] |
| - | [[Category: Ciulli, A]] | + | [[Category: Ciulli A]] |
| - | [[Category: Lobley, C M.C]] | + | [[Category: Lobley CMC]] |
| - | [[Category: Smith, A G]] | + | [[Category: Smith AG]] |
| - | [[Category: Whitney, H M]] | + | [[Category: Whitney HM]] |
| - | [[Category: Williams, G]] | + | [[Category: Williams G]] |
| - | [[Category: Ketopantoate]]
| + | |
| - | [[Category: Nadp+ dependent]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pantothenate pathway]]
| + | |
| - | [[Category: Secondary alcohol dehydrogenase]]
| + | |
| Structural highlights
Function
PANE_ECOLI Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
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
The NADPH-dependent reduction of ketopantoate to pantoate, catalyzed by ketopantoate reductase (KPR; EC 1.1.1.169), is essential for the biosynthesis of pantothenate (vitamin B(5)). Here we present the crystal structure of Escherichia coli KPR with NADP(+) bound, solved to 2.1 A resolution. The cofactor is bound in the active site cleft between the N-terminal Rossmann-fold domain and the C-terminal alpha-helical domain. The thermodynamics of cofactor and substrate binding were characterized by isothermal titration calorimetry. The dissociation constant for NADP(+) was found to be 6.5 muM, 20-fold larger than that for NADPH (0.34 muM). The difference is primarily due to the entropic term, suggesting favorable hydrophobic interactions of the more lipophilic nicotinamide ring in NADPH. Comparison of this binary complex structure with the previously studied apoenzyme reveals no evidence for large domain movements on cofactor binding. This observation is further supported both by molecular dynamics and by calorimetric analysis. A model of the ternary complex, based on the structure presented here, provides novel insights into the molecular mechanism of enzyme catalysis. We propose a conformational switch of the essential Lys176 from the "resting" state observed in our structure to an "active" state, to bind ketopantoate. Additionally, we identify the importance of Asn98 for substrate binding and enzyme catalysis.
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound.,Lobley CM, Ciulli A, Whitney HM, Williams G, Smith AG, Abell C, Blundell TL Biochemistry. 2005 Jun 28;44(25):8930-9. PMID:15966718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lobley CM, Ciulli A, Whitney HM, Williams G, Smith AG, Abell C, Blundell TL. The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. Biochemistry. 2005 Jun 28;44(25):8930-9. PMID:15966718 doi:10.1021/bi0502036
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