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| | ==Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with CoA== | | ==Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with CoA== |
| - | <StructureSection load='4dpm' size='340' side='right' caption='[[4dpm]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='4dpm' size='340' side='right'caption='[[4dpm]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dpm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DPM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dpm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DPM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dpk|4dpk]], [[4dpl|4dpl]]</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=4dpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpm OCA], [https://pdbe.org/4dpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dpm RCSB], [https://www.ebi.ac.uk/pdbsum/4dpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mcr/scr, STK_21710 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
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| - | <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=4dpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpm OCA], [http://pdbe.org/4dpm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dpm RCSB], [http://www.ebi.ac.uk/pdbsum/4dpm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCR_SULTO MCR_SULTO]] Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. Can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.<ref>PMID:17041055</ref> | + | [[https://www.uniprot.org/uniprot/MCR_SULTO MCR_SULTO]] Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. Can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.<ref>PMID:17041055</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sulto]] | + | [[Category: Large Structures]] |
| - | [[Category: Demmer, U]] | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Ermler, U]] | + | [[Category: Demmer U]] |
| - | [[Category: Fuchs, G]] | + | [[Category: Ermler U]] |
| - | [[Category: Kockelkorn, D]] | + | [[Category: Fuchs G]] |
| - | [[Category: Srivastava, A]] | + | [[Category: Kockelkorn D]] |
| - | [[Category: Warkentin, E]] | + | [[Category: Srivastava A]] |
| - | [[Category: Coa]]
| + | [[Category: Warkentin E]] |
| - | [[Category: Dimerization domain]]
| + | |
| - | [[Category: Dinucleotide binding]]
| + | |
| - | [[Category: Nadp]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Reductase]]
| + | |
| Structural highlights
Function
[MCR_SULTO] Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. Can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.[1]
Publication Abstract from PubMed
Autotrophic members of the Sulfolobales (crenarchaeota) use the 3-hydroxypropionate/4-hydroxybutyrate cycle to assimilate CO2 into cell material. The product of the initial acetyl-CoA carboxylation with CO2, malonyl-CoA, is further reduced to malonic semialdehyde by an NADPH-dependent malonyl-CoA reductase (MCR); the enzyme also catalyzes the reduction of succinyl-CoA to succinic semialdehyde onwards in the cycle. Here, we present the crystal structure of Sulfolobus tokodaii malonyl-CoA reductase in the substrate-free state and in complex with NADP+ and CoA. Structural analysis revealed an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites. Both coenzymes are pressed into a S-shaped, nearly superimposable structure imposed by a fixed and preformed binding site. The template-governed cofactor shaping implicates the same binding site for the 3- and 2- ribose phosphate group of CoA and NADP+, respectively, but a different one for the common ADP part: the beta-phosphate of CoA aligns with the alpha-phosphate of NADP+. Evolution from an NADP+ to a bispecific NADP+ and CoA binding site involves many amino acid exchanges within a complex process by which constraints of the CoA structure also influence NADP+ binding. Based on the paralogous aspartate-semialdehyde dehydrogenase structurally characterized with a covalent Cys-aspartyl adduct, a malonyl/succinyl group can be reliably modelled into MCR and discussed regarding its binding mode, the malonyl/succinyl specificity, and the catalyzed reaction. The modified polypeptide surrounding around the absent ammonium group in malonate/succinate compared to aspartate provides the structural basis for engineering a methylmalonyl-CoA reductase applied for biotechnical polyester building block synthesis.
Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase.,Demmer U, Warkentin E, Srivastava A, Kockelkorn D, Poetter M, Marx A, Fuchs G, Ermler U J Biol Chem. 2013 Jan 16. PMID:23325803[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alber B, Olinger M, Rieder A, Kockelkorn D, Jobst B, Hugler M, Fuchs G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J Bacteriol. 2006 Dec;188(24):8551-9. Epub 2006 Oct 13. PMID:17041055 doi:http://dx.doi.org/10.1128/JB.00987-06
- ↑ Demmer U, Warkentin E, Srivastava A, Kockelkorn D, Poetter M, Marx A, Fuchs G, Ermler U. Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase. J Biol Chem. 2013 Jan 16. PMID:23325803 doi:http://dx.doi.org/10.1074/jbc.M112.421263
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