8rth
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Trypanosoma brucei 3-methylcrotonyl-CoA carboxylase== | |
| + | <StructureSection load='8rth' size='340' side='right'caption='[[8rth]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8rth]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RTH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.37Å</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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8rth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rth OCA], [https://pdbe.org/8rth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rth RCSB], [https://www.ebi.ac.uk/pdbsum/8rth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rth ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q57YQ4_TRYB2 Q57YQ4_TRYB2] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 3-Methylcrotonyl-CoA carboxylase (MCC) catalyzes the two-step, biotin-dependent production of 3-methylglutaconyl-CoA, an essential intermediate in leucine catabolism. Given the critical metabolic role of MCC, deficiencies in this enzyme lead to organic aciduria, while its overexpression is linked to tumor development. MCC is a dodecameric enzyme composed of six copies of each alpha- and beta-subunit. We present the cryo-EM structure of the endogenous MCC holoenzyme from Trypanosoma brucei in a non-filamentous state at 2.4 A resolution. Biotin is covalently bound to the biotin carboxyl carrier protein domain of alpha-subunits and positioned in a non-canonical pocket near the active site of neighboring beta-subunit dimers. Moreover, flexibility of key residues at alpha-subunit interfaces and loops enables pivoting of alpha-subunit trimers to partly reduce the distance between alpha- and beta-subunit active sites, required for MCC catalysis. Our results provide a structural framework to understand the enzymatic mechanism of eukaryotic MCCs and to assist drug discovery against trypanosome infections. | ||
| - | + | The cryo-EM structure of trypanosome 3-methylcrotonyl-CoA carboxylase provides mechanistic and dynamic insights into its enzymatic function.,Plaza-Pegueroles A, Aphasizheva I, Aphasizhev R, Fernandez-Tornero C, Ruiz FM Structure. 2024 Jul 11;32(7):930-940.e3. doi: 10.1016/j.str.2024.03.010. Epub , 2024 Apr 8. PMID:38593794<ref>PMID:38593794</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8rth" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Trypanosoma brucei]] | ||
| + | [[Category: Fernandez-Tornero C]] | ||
| + | [[Category: Plaza-Pegueroles A]] | ||
| + | [[Category: Ruiz FM]] | ||
Current revision
Trypanosoma brucei 3-methylcrotonyl-CoA carboxylase
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