4dpl: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP== | ==Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP== | ||
<StructureSection load='4dpl' size='340' side='right' caption='[[4dpl]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4dpl' size='340' side='right'caption='[[4dpl]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4dpl]] is a 4 chain structure with sequence from [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <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></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'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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 == | ||
| Line 24: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Demmer | [[Category: Sulfurisphaera tokodaii str. 7]] | ||
[[Category: Ermler | [[Category: Demmer U]] | ||
[[Category: Fuchs | [[Category: Ermler U]] | ||
[[Category: Kockelkorn | [[Category: Fuchs G]] | ||
[[Category: Srivastava | [[Category: Kockelkorn D]] | ||
[[Category: Warkentin | [[Category: Srivastava A]] | ||
[[Category: Warkentin E]] | |||
Latest revision as of 12:56, 30 October 2024
Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadPStructure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP
Structural highlights
FunctionMCR_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 PubMedAutotrophic 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
|
| ||||||||||||||||||