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8i6z
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of apo-form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus== | |
| + | <StructureSection load='8i6z' size='340' side='right'caption='[[8i6z]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8i6z]] 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=8I6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I6Z 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=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=8i6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i6z OCA], [https://pdbe.org/8i6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i6z RCSB], [https://www.ebi.ac.uk/pdbsum/8i6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i6z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A9WIU3_CHLAA A9WIU3_CHLAA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 May 3;242(Pt 1):124676. doi: , 10.1016/j.ijbiomac.2023.124676. PMID:37146856<ref>PMID:37146856</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Kim | + | <div class="pdbe-citations 8i6z" style="background-color:#fffaf0;"></div> |
| - | [[Category: Kim | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chloroflexus aurantiacus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim K-J]] | ||
| + | [[Category: Kim S]] | ||
Revision as of 08:20, 14 June 2023
Crystal structure of apo-form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus
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