8f41

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Current revision (06:41, 19 June 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8f41]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_tarentolae Leishmania tarentolae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F41 FirstGlance]. <br>
<table><tr><td colspan='2'>[[8f41]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_tarentolae Leishmania tarentolae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F41 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</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=8f41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f41 OCA], [https://pdbe.org/8f41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f41 RCSB], [https://www.ebi.ac.uk/pdbsum/8f41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f41 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=8f41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f41 OCA], [https://pdbe.org/8f41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f41 RCSB], [https://www.ebi.ac.uk/pdbsum/8f41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f41 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/A0A640KPA4_LEITA A0A640KPA4_LEITA]
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[https://www.uniprot.org/uniprot/A0A640KGP9_LEITA A0A640KGP9_LEITA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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3-methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent mitochondrial enzyme necessary for leucine catabolism in most organisms. While the crystal structure of recombinant bacterial MCC has been characterized, the structure and potential polymerization of native MCC remain elusive. Here, we discovered that native MCC from Leishmania tarentolae (LtMCC) forms filaments, and determined the structures of different filament regions at 3.4, 3.9, and 7.3 A resolution using cryoEM. alpha(6)beta(6) LtMCCs assemble in a twisted-stacks architecture, manifesting as supramolecular rods up to 400 nm. Filamentous LtMCCs bind biotin non-covalently and lack coenzyme A. Filaments elongate by stacking alpha(6)beta(6) LtMCCs onto the exterior alpha-trimer of the terminal LtMCC. This stacking immobilizes the biotin carboxylase domains, sequestering the enzyme in an inactive state. Our results support a new model for LtMCC catalysis, termed the dual-swinging-domains model, and cast new light on the function of polymerization in the carboxylase superfamily and beyond.
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Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.,Hu JJ, Lee JKJ, Liu YT, Yu C, Huang L, Aphasizheva I, Aphasizhev R, Zhou ZH Structure. 2023 Jan 5;31(1):100-110.e4. doi: 10.1016/j.str.2022.11.015. Epub 2022 , Dec 20. PMID:36543169<ref>PMID:36543169</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8f41" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

3-methylcrotonyl-CoA carboxylase in filament, alpha-subunit centered

PDB ID 8f41

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