6kin: Difference between revisions
New page: '''Unreleased structure''' The entry 6kin is ON HOLD Authors: Tang, W.R., Zhang, C.Y., Wang, C., Xu, X.L. Description: Crystal structure of the tri-functional malyl-CoA lyase from Rose... |
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==Crystal structure of the tri-functional malyl-CoA lyase from Roseiflexus castenholzii== | |||
<StructureSection load='6kin' size='340' side='right'caption='[[6kin]], [[Resolution|resolution]] 2.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6kin]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseiflexus_castenholzii_DSM_13941 Roseiflexus castenholzii DSM 13941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KIN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.527Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=6kin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kin OCA], [https://pdbe.org/6kin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kin RCSB], [https://www.ebi.ac.uk/pdbsum/6kin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kin ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A7NHT0_ROSCS A7NHT0_ROSCS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Malyl-coenzyme A lyase (MCL) is a carbon-carbon bond lyase that catalyzes the reversible cleavage of coenzyme A (CoA) thioesters in multiple carbon metabolic pathways. This enzyme contains a CitE-like TIM barrel and an additional C-terminal domain that undergoes conformational changes upon substrate binding. However, the structural basis underlying these conformational changes is elusive. Here, we report the crystal structure of MCL from the thermophilic photosynthetic bacterium Roseiflexus castenholzii (RfxMCL) in the apo- and oxalate-bound forms at resolutions of 2.50 and 2.65â¯A, respectively. Molecular dynamics simulations and structural comparisons with MCLs from other species reveal the deflection of the C-terminal domain to close the adjacent active site pocket in the trimer and contribute active site residues for CoA coordination. The deflection angles of the C-terminal domain are not only related to the occupation but also the type of bound substrates in the adjacent active site pocket. Our work illustrates that a conformational switch of the C-terminal domain accompanies the substrate-binding of MCLs. The results provide a framework for further investigating the reaction mechanism and multifunctionality of MCLs in different carbon metabolic pathways. | |||
The C-terminal domain conformational switch revealed by the crystal structure of malyl-CoA lyase from Roseiflexus castenholzii.,Tang W, Wang Z, Zhang C, Wang C, Min Z, Zhang X, Liu D, Shen J, Xu X Biochem Biophys Res Commun. 2019 Oct 8;518(1):72-79. doi: , 10.1016/j.bbrc.2019.08.010. Epub 2019 Aug 9. PMID:31405562<ref>PMID:31405562</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6kin" style="background-color:#fffaf0;"></div> | ||
[[Category: Tang | |||
[[Category: Wang | ==See Also== | ||
[[Category: Zhang | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Roseiflexus castenholzii DSM 13941]] | |||
[[Category: Tang WR]] | |||
[[Category: Wang C]] | |||
[[Category: Xu XL]] | |||
[[Category: Zhang CY]] | |||
Latest revision as of 13:34, 22 November 2023
Crystal structure of the tri-functional malyl-CoA lyase from Roseiflexus castenholziiCrystal structure of the tri-functional malyl-CoA lyase from Roseiflexus castenholzii
Structural highlights
FunctionPublication Abstract from PubMedMalyl-coenzyme A lyase (MCL) is a carbon-carbon bond lyase that catalyzes the reversible cleavage of coenzyme A (CoA) thioesters in multiple carbon metabolic pathways. This enzyme contains a CitE-like TIM barrel and an additional C-terminal domain that undergoes conformational changes upon substrate binding. However, the structural basis underlying these conformational changes is elusive. Here, we report the crystal structure of MCL from the thermophilic photosynthetic bacterium Roseiflexus castenholzii (RfxMCL) in the apo- and oxalate-bound forms at resolutions of 2.50 and 2.65â¯A, respectively. Molecular dynamics simulations and structural comparisons with MCLs from other species reveal the deflection of the C-terminal domain to close the adjacent active site pocket in the trimer and contribute active site residues for CoA coordination. The deflection angles of the C-terminal domain are not only related to the occupation but also the type of bound substrates in the adjacent active site pocket. Our work illustrates that a conformational switch of the C-terminal domain accompanies the substrate-binding of MCLs. The results provide a framework for further investigating the reaction mechanism and multifunctionality of MCLs in different carbon metabolic pathways. The C-terminal domain conformational switch revealed by the crystal structure of malyl-CoA lyase from Roseiflexus castenholzii.,Tang W, Wang Z, Zhang C, Wang C, Min Z, Zhang X, Liu D, Shen J, Xu X Biochem Biophys Res Commun. 2019 Oct 8;518(1):72-79. doi: , 10.1016/j.bbrc.2019.08.010. Epub 2019 Aug 9. PMID:31405562[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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