|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <SX load='4v8l' size='340' side='right' viewer='molstar' caption='[[4v8l]], [[Resolution|resolution]] 7.50Å' scene=''> | | <SX load='4v8l' size='340' side='right' viewer='molstar' caption='[[4v8l]], [[Resolution|resolution]] 7.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v8l]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3zen 3zen] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4b3y 4b3y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4V8L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v8l]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3zen 3zen] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4b3y 4b3y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V8L FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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://proteopedia.org/fgij/fg.htm?mol=4v8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8l OCA], [http://pdbe.org/4v8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v8l RCSB], [http://www.ebi.ac.uk/pdbsum/4v8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v8l 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=4v8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8l OCA], [https://pdbe.org/4v8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v8l RCSB], [https://www.ebi.ac.uk/pdbsum/4v8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v8l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0R1H7_MYCS2 A0R1H7_MYCS2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 27: |
| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycobacterium smegmatis]] | + | [[Category: Mycolicibacterium smegmatis]] |
| - | [[Category: Ban, N]] | + | [[Category: Ban N]] |
| - | [[Category: Boehringer, D]] | + | [[Category: Boehringer D]] |
| - | [[Category: Leibundgut, M]] | + | [[Category: Leibundgut M]] |
| - | [[Category: Multifunctional enzyme]]
| + | |
| - | [[Category: Mycolic acid biosynthesis]]
| + | |
| - | [[Category: Substrate channeling]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0R1H7_MYCS2
Publication Abstract from PubMed
The mycobacterial fatty acid synthase (FAS) complex is a giant 2.0-MDa alpha(6) homohexameric multifunctional enzyme that catalyzes synthesis of fatty acid precursors of mycolic acids, which are major components of the cell wall in Mycobacteria and play an important role in pathogenicity. Here, we present a three-dimensional reconstruction of the Mycobacterium smegmatis FAS complex at 7.5A, highly homologous to the Mycobacterium tuberculosis multienzyme, by cryo-electron microscopy. Based on the obtained structural data, which allowed us to identify secondary-structure elements, and sequence homology with the fungal FAS, we generated an accurate architectural model of the complex. The FAS system from Mycobacteria resembles a minimized version of the fungal FAS with much larger openings in the reaction chambers. These architectural features of the mycobacterial FAS may be important for the interaction with mycolic acid processing and condensing enzymes that further modify the precursors produced by FAS and for autoactivation of the FAS complex.
7.5-A Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase.,Boehringer D, Ban N, Leibundgut M J Mol Biol. 2013 Jan 3. pii: S0022-2836(12)00969-2. doi:, 10.1016/j.jmb.2012.12.021. PMID:23291528[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boehringer D, Ban N, Leibundgut M. 7.5-A Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase. J Mol Biol. 2013 Jan 3. pii: S0022-2836(12)00969-2. doi:, 10.1016/j.jmb.2012.12.021. PMID:23291528 doi:http://dx.doi.org/10.1016/j.jmb.2012.12.021
|
