|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <SX load='4v8v' size='340' side='right' viewer='molstar' caption='[[4v8v]], [[Resolution|resolution]] 20.00Å' scene=''> | | <SX load='4v8v' size='340' side='right' viewer='molstar' caption='[[4v8v]], [[Resolution|resolution]] 20.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v8v]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bjd 4bjd] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bje 4bje]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V8V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v8v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bjd 4bjd] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bje 4bje]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V8V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 20Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bjf|4bjf]], [[4bjg|4bjg]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8v OCA], [http://pdbe.org/4v8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v8v RCSB], [http://www.ebi.ac.uk/pdbsum/4v8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v8v 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=4v8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8v OCA], [https://pdbe.org/4v8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v8v RCSB], [https://www.ebi.ac.uk/pdbsum/4v8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v8v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 22: |
Line 22: |
| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ciccarelli, L]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Connell, S R]] | + | [[Category: Ciccarelli L]] |
| - | [[Category: Enderle, M]] | + | [[Category: Connell SR]] |
| - | [[Category: Grininger, M]] | + | [[Category: Enderle M]] |
| - | [[Category: Mills, D J]] | + | [[Category: Grininger M]] |
| - | [[Category: Vonck, J]] | + | [[Category: Mills DJ]] |
| - | [[Category: Codimensional principal component analysis]]
| + | [[Category: Vonck J]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Antibiotic therapy in response to Mycobacterium tuberculosis infections targets de novo fatty acid biosynthesis, which is orchestrated by a 1.9 MDa type I fatty acid synthase (FAS). Here, we characterize M. tuberculosis FAS by single-particle cryo-electron microscopy and interpret the data by docking the molecular models of yeast and Mycobacterium smegmatis FAS. Our analysis reveals a porous barrel-like structure of considerable conformational variability that is illustrated by the identification of several conformational states with altered topology in the multienzymatic assembly. This demonstrates that the barrel-like structure of M. tuberculosis FAS is not just a static scaffold for the catalytic domains, but may play an active role in coordinating fatty acid synthesis. The conception of M. tuberculosis FAS as a highly dynamic assembly of domains revises the view on bacterial type I fatty acid synthesis and might inspire new strategies for inhibition of de novo fatty acid synthesis in M. tuberculosis.
Structure and Conformational Variability of the Mycobacterium tuberculosis Fatty Acid Synthase Multienzyme Complex.,Ciccarelli L, Connell SR, Enderle M, Mills DJ, Vonck J, Grininger M Structure. 2013 Jun 5. pii: S0969-2126(13)00153-6. doi:, 10.1016/j.str.2013.04.023. PMID:23746808[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ciccarelli L, Connell SR, Enderle M, Mills DJ, Vonck J, Grininger M. Structure and Conformational Variability of the Mycobacterium tuberculosis Fatty Acid Synthase Multienzyme Complex. Structure. 2013 Jun 5. pii: S0969-2126(13)00153-6. doi:, 10.1016/j.str.2013.04.023. PMID:23746808 doi:10.1016/j.str.2013.04.023
|
