7cz3: Difference between revisions
New page: '''Unreleased structure''' The entry 7cz3 is ON HOLD until Paper Publication Authors: Park, J., Kim, K.-J. Description: Crystal strcuture of Acyl-CoA thioesterase from Bacillus cereus ... |
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==Crystal strcuture of Acyl-CoA thioesterase from Bacillus cereus ATCC 14579== | |||
<StructureSection load='7cz3' size='340' side='right'caption='[[7cz3]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7cz3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CZ3 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=7cz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cz3 OCA], [https://pdbe.org/7cz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cz3 RCSB], [https://www.ebi.ac.uk/pdbsum/7cz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cz3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q814K4_BACCR Q814K4_BACCR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Acyl-CoA thioesterase is an enzyme that catalyzes the cleavage of thioester bonds and regulates the cellular concentrations of CoASH, fatty acids, and acyl-CoA. In this study, we report the crystal structure of acyl-CoA thioesterase from Bacillus cereus ATCC 14579 (BcACT1) complexed with the CoA product. BcACT1 possesses a monomeric structure of a hotdog-fold and forms a hexamer via the trimerization of three dimers. We identified the active site of BcACT1 and revealed that residues Asn23 and Asp38 are crucial for enzyme catalysis, indicating that BcACT1 belongs to the TE6 family. We also propose that BcACT1 might undergo an open-closed conformational change on the acyl-CoA binding pocket upon binding of the acyl-CoA substrate. Interestingly, the BcACT1 variants with dramatically increased activities were obtained during the site-directed mutagenesis experiments to confirm the residues involved in CoA binding. Finally, we found that BcACT1 is not nucleotide-regulated and suggest that the length and shape of the additional alpha2-helix are crucial in determining a regulation mode by nucleotides. | |||
Structural basis for nucleotide-independent regulation of acyl-CoA thioesterase from Bacillus cereus ATCC 14579.,Park J, Kim YJ, Lee D, Kim KJ Int J Biol Macromol. 2020 Dec 28;170:390-396. doi:, 10.1016/j.ijbiomac.2020.12.174. PMID:33383082<ref>PMID:33383082</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Kim | <div class="pdbe-citations 7cz3" style="background-color:#fffaf0;"></div> | ||
[[Category: Park | |||
==See Also== | |||
*[[Thioesterase 3D structures|Thioesterase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus cereus ATCC 14579]] | |||
[[Category: Large Structures]] | |||
[[Category: Kim K-J]] | |||
[[Category: Park J]] | |||
Latest revision as of 19:20, 29 November 2023
Crystal strcuture of Acyl-CoA thioesterase from Bacillus cereus ATCC 14579Crystal strcuture of Acyl-CoA thioesterase from Bacillus cereus ATCC 14579
Structural highlights
FunctionPublication Abstract from PubMedAcyl-CoA thioesterase is an enzyme that catalyzes the cleavage of thioester bonds and regulates the cellular concentrations of CoASH, fatty acids, and acyl-CoA. In this study, we report the crystal structure of acyl-CoA thioesterase from Bacillus cereus ATCC 14579 (BcACT1) complexed with the CoA product. BcACT1 possesses a monomeric structure of a hotdog-fold and forms a hexamer via the trimerization of three dimers. We identified the active site of BcACT1 and revealed that residues Asn23 and Asp38 are crucial for enzyme catalysis, indicating that BcACT1 belongs to the TE6 family. We also propose that BcACT1 might undergo an open-closed conformational change on the acyl-CoA binding pocket upon binding of the acyl-CoA substrate. Interestingly, the BcACT1 variants with dramatically increased activities were obtained during the site-directed mutagenesis experiments to confirm the residues involved in CoA binding. Finally, we found that BcACT1 is not nucleotide-regulated and suggest that the length and shape of the additional alpha2-helix are crucial in determining a regulation mode by nucleotides. Structural basis for nucleotide-independent regulation of acyl-CoA thioesterase from Bacillus cereus ATCC 14579.,Park J, Kim YJ, Lee D, Kim KJ Int J Biol Macromol. 2020 Dec 28;170:390-396. doi:, 10.1016/j.ijbiomac.2020.12.174. PMID:33383082[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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