8i70
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8i70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I70 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8i70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I70 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 1.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=8i70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i70 OCA], [https://pdbe.org/8i70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i70 RCSB], [https://www.ebi.ac.uk/pdbsum/8i70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i70 ProSAT]</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=8i70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i70 OCA], [https://pdbe.org/8i70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i70 RCSB], [https://www.ebi.ac.uk/pdbsum/8i70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i70 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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The platform chemical 3-hydroxypropionic acid is used to synthesize various valuable materials, including bioplastics. Bifunctional malonyl-CoA reductase is a key enzyme in 3-hydroxypropionic acid biosynthesis as it catalyzes the two-step reduction of malonyl-CoA to malonate semialdehyde to 3-hydroxypropionic acid. Here, we report the cryo-EM structure of a full-length malonyl-CoA reductase protein from Chloroflexus aurantiacus (CaMCR(Full)). The EM model of CaMCR(Full) reveals a tandem helix architecture comprising an N-terminal (CaMCR(ND)) and a C-terminal (CaMCR(CD)) domain. The CaMCR(Full) model also revealed that the enzyme undergoes a dynamic domain movement between CaMCR(ND) and CaMCR(CD) due to the presence of a flexible linker between these two domains. Increasing the flexibility and extension of the linker resulted in a twofold increase in enzyme activity, indicating that for CaMCR, domain movement is crucial for high enzyme activity. We also describe the structural features of CaMCR(ND) and CaMCR(CD). This study reveals the protein structures underlying the molecular mechanism of CaMCR(Full) and thereby provides valuable information for future enzyme engineering to improve the productivity of 3-hydroxypropionic acid. | The platform chemical 3-hydroxypropionic acid is used to synthesize various valuable materials, including bioplastics. Bifunctional malonyl-CoA reductase is a key enzyme in 3-hydroxypropionic acid biosynthesis as it catalyzes the two-step reduction of malonyl-CoA to malonate semialdehyde to 3-hydroxypropionic acid. Here, we report the cryo-EM structure of a full-length malonyl-CoA reductase protein from Chloroflexus aurantiacus (CaMCR(Full)). The EM model of CaMCR(Full) reveals a tandem helix architecture comprising an N-terminal (CaMCR(ND)) and a C-terminal (CaMCR(CD)) domain. The CaMCR(Full) model also revealed that the enzyme undergoes a dynamic domain movement between CaMCR(ND) and CaMCR(CD) due to the presence of a flexible linker between these two domains. Increasing the flexibility and extension of the linker resulted in a twofold increase in enzyme activity, indicating that for CaMCR, domain movement is crucial for high enzyme activity. We also describe the structural features of CaMCR(ND) and CaMCR(CD). This study reveals the protein structures underlying the molecular mechanism of CaMCR(Full) and thereby provides valuable information for future enzyme engineering to improve the productivity of 3-hydroxypropionic acid. | ||
| - | Cryo-EM structure of bifunctional malonyl-CoA reductase from Chloroflexus aurantiacus reveals a dynamic domain movement for high enzymatic activity.,Ahn JW, Kim S, Hong J, Kim KJ Int J Biol Macromol. 2023 | + | Cryo-EM structure of bifunctional malonyl-CoA reductase from Chloroflexus aurantiacus reveals a dynamic domain movement for high enzymatic activity.,Ahn JW, Kim S, Hong J, Kim KJ Int J Biol Macromol. 2023 Jul 1;242(Pt 1):124676. doi: , 10.1016/j.ijbiomac.2023.124676. Epub 2023 May 3. PMID:37146856<ref>PMID:37146856</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Crystal structure of NADP-binding form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus
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