|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5e4r' size='340' side='right'caption='[[5e4r]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='5e4r' size='340' side='right'caption='[[5e4r]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ignaa Ignaa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E4R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ignisphaera_aggregans_DSM_17230 Ignisphaera aggregans DSM 17230]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E4R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.94Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ilvC, Igag_1561 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=583356 IGNAA])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </span></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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [https://pdbe.org/5e4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [https://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r ProSAT]</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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ILVC_IGNAA ILVC_IGNAA] Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate.<ref>PMID:25172159</ref> <ref>PMID:26644020</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ignaa]] | + | [[Category: Ignisphaera aggregans DSM 17230]] |
| - | [[Category: Ketol-acid reductoisomerase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arnold, F H]] | + | [[Category: Arnold FH]] |
| - | [[Category: Brinkmann-Chen, S]] | + | [[Category: Brinkmann-Chen S]] |
| - | [[Category: Buller, A R]] | + | [[Category: Buller AR]] |
| - | [[Category: Cahn, J K.B]] | + | [[Category: Cahn JKB]] |
| - | [[Category: Chimera protein]]
| + | |
| - | [[Category: Ketol-acid reductiosomerase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Protein engineering]]
| + | |
| - | [[Category: Protein knot]]
| + | |
| - | [[Category: Psuedodimer]]
| + | |
| Structural highlights
5e4r is a 1 chain structure with sequence from Ignisphaera aggregans DSM 17230. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.94Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ILVC_IGNAA Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate.[1] [2]
Publication Abstract from PubMed
The duplication of protein structural domains has been proposed as a common mechanism for the generation of new protein folds. A particularly interesting case is the class II ketol-acid reductoisomerase (KARI), which putatively arose from an ancestral class I KARI by duplication of the C-terminal domain and corresponding loss of obligate dimerization. As a result, the class II enzymes acquired a deeply embedded figure-of-eight knot. To test this evolutionary hypothesis we constructed a novel class II KARI by duplicating the C-terminal domain of a hyperthermostable class I KARI. The new protein is monomeric, as confirmed by gel filtration and x-ray crystallography, and has the deeply-knotted class II KARI fold. Surprisingly, its catalytic activity is nearly unchanged from the parent KARI. This provides strong evidence in support of domain duplication as the mechanism for the evolution of the class II KARI fold and demonstrates the ability of domain duplication to generate topological novelty in a function-neutral manner. This article is protected by copyright. All rights reserved.
Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases.,Cahn JK, Brinkmann-Chen S, Buller AR, Arnold FH Protein Sci. 2015 Dec 8. doi: 10.1002/pro.2852. PMID:26644020[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brinkmann-Chen S, Cahn JK, Arnold FH. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab Eng. 2014 Aug 27;26C:17-22. doi: 10.1016/j.ymben.2014.08.003. PMID:25172159 doi:http://dx.doi.org/10.1016/j.ymben.2014.08.003
- ↑ Cahn JK, Brinkmann-Chen S, Buller AR, Arnold FH. Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases. Protein Sci. 2015 Dec 8. doi: 10.1002/pro.2852. PMID:26644020 doi:http://dx.doi.org/10.1002/pro.2852
- ↑ Cahn JK, Brinkmann-Chen S, Buller AR, Arnold FH. Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases. Protein Sci. 2015 Dec 8. doi: 10.1002/pro.2852. PMID:26644020 doi:http://dx.doi.org/10.1002/pro.2852
|
