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4dpl

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Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP

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 ==Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP==
-<StructureSection load='4dpl' size='340' side='right' caption='[[4dpl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='4dpl' size='340' side='right'caption='[[4dpl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4dpl]] is a 4 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=4DPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DPL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4dpl]] is a 4 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=4DPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DPL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dpk|4dpk]], [[4dpm|4dpm]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpl OCA], [https://pdbe.org/4dpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dpl RCSB], [https://www.ebi.ac.uk/pdbsum/4dpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpl ProSAT]</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=4dpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpl OCA], [http://pdbe.org/4dpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dpl RCSB], [http://www.ebi.ac.uk/pdbsum/4dpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpl ProSAT]</span></td></tr>
 </table>
 == 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;">
-== 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<ref>PMID:23325803</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4dpl" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </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]]

4dpl

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Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP

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