4dpm: Difference between revisions

<StructureSection load='4dpm' size='340' side='right' caption='[[4dpm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<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>

</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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dpk|4dpk]], [[4dpl|4dpl]]</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'>[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://www.rcsb.org/pdb/explore.do?structureId=4dpm RCSB], [http://www.ebi.ac.uk/pdbsum/4dpm PDBsum]</span></td></tr>

== 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>

 

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[[Category: Sulto]]

[[Category: Demmer, U]]

[[Category: Ermler, U]]

[[Category: Fuchs, G]]

[[Category: Kockelkorn, D]]

[[Category: Srivastava, A]]

[[Category: Warkentin, E]]

[[Category: Reductase]]