9tqc: Difference between revisions
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==L. pneumophila 3-methylcrotonyl-CoA carboxylase holoenzyme A3B6== | |||
<StructureSection load='9tqc' size='340' side='right'caption='[[9tqc]], [[Resolution|resolution]] 2.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9tqc]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9TQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9TQC 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]] 2.48Å</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=9tqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9tqc OCA], [https://pdbe.org/9tqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9tqc RCSB], [https://www.ebi.ac.uk/pdbsum/9tqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9tqc ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
3-Methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent carboxylase that metabolizes the amino acid leucine. MCC is present in bacteria, fungi, plants, and animals. In humans, its overexpression is linked to cancer, and its deficiency is linked to inborn errors of metabolism with severe consequences, so understanding its structure and function has far reaching implications. Here, we explore the MCC from Legionella pneumophila, a pathogenic bacterium with a biphasic life cycle. Our endogenous holoenzyme yielded the highest resolution cryo-EM structure of MCC to date, allowing for identification of protein components by the machine learning tool ModelAngelo, confirmed independently by mass spectrometry. We also observed, for the first time, enhanced filamentation of MCC upon substrate binding. We propose that this filamentation, previously observed in the eukaryotes, but not in bacteria, may be important for cellular processes such as differentiation of life cycle or cell division. | |||
Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase in Legionella pneumophila.,Somarathne RP, Shrestha R, Zehra M, Brodeur C, Bhella D, Lai WC, Meir A, Durie CL bioRxiv [Preprint]. 2025 Dec 23:2025.12.22.694428. doi: , 10.64898/2025.12.22.694428. PMID:41509382<ref>PMID:41509382</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9tqc" style="background-color:#fffaf0;"></div> | ||
[[Category: Bhella | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Legionella pneumophila]] | ||
[[Category: | [[Category: Bhella D]] | ||
[[Category: Brodeur C]] | |||
[[Category: Durie C]] | |||
[[Category: Lai WC]] | |||
[[Category: Meir A]] | |||
[[Category: Shrestha R]] | |||
[[Category: Somarathne R]] | |||
[[Category: Zehra M]] | |||
