3zen
From Proteopedia
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- | [[ | + | ==Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase== |
+ | <StructureSection load='3zen' size='340' side='right' caption='[[3zen]], [[Resolution|resolution]] 7.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3zen]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZEN 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> | ||
+ | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b3y|4b3y]]</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=3zen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zen OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zen RCSB], [http://www.ebi.ac.uk/pdbsum/3zen PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:23291528</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Fatty acid synthase|Fatty acid synthase]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Mycobacterium smegmatis]] | [[Category: Mycobacterium smegmatis]] | ||
- | [[Category: Ban, N | + | [[Category: Ban, N]] |
- | [[Category: Boehringer, D | + | [[Category: Boehringer, D]] |
- | [[Category: Leibundgut, M | + | [[Category: Leibundgut, M]] |
[[Category: Multifunctional enzyme]] | [[Category: Multifunctional enzyme]] | ||
[[Category: Mycolic acid biosynthesis]] | [[Category: Mycolic acid biosynthesis]] | ||
[[Category: Substrate channeling]] | [[Category: Substrate channeling]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 16:51, 9 December 2014
Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase
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