3hmj
From Proteopedia
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| - | {{Large structure}} | ||
| - | {{STRUCTURE_3hmj| PDB=3hmj | SCENE= }} | ||
| - | ===Saccharomyces cerevisiae FAS type I=== | ||
| - | {{ABSTRACT_PUBMED_19679086}} | ||
| - | == | + | ==Saccharomyces cerevisiae FAS type I== |
| - | [[3hmj]] is a 6 chain structure with sequence from [ | + | <StructureSection load='3hmj' size='340' side='right'caption='[[3hmj]], [[Resolution|resolution]] 4.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3hmj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HMJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=3hmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hmj OCA], [https://pdbe.org/3hmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hmj RCSB], [https://www.ebi.ac.uk/pdbsum/3hmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hmj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/3hmj_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hmj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT). However, recent X-ray structures of the fungal FAS revealed a barrel-shaped architecture, with PPT located at the outside of the barrel wall, spatially separated from the ACP caged in the inner volume. This separation indicated that the activation has to proceed before the assembly to the mature complex, in a conformation where the ACP and PPT domains can meet. To gain insight into the auto-activation reaction and also into the fungal FAS assembly pathway, we structurally and functionally characterized the Saccharomyces cerevisiae FAS type I PPT as part of the multienzyme protein and as an isolated domain. | ||
| - | + | Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.,Johansson P, Mulinacci B, Koestler C, Vollrath R, Oesterhelt D, Grininger M Structure. 2009 Aug 12;17(8):1063-74. PMID:19679086<ref>PMID:19679086</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 3hmj" style="background-color:#fffaf0;"></div> |
| + | |||
| + | ==See Also== | ||
| + | *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Grininger | + | [[Category: Grininger M]] |
| - | [[Category: Johansson | + | [[Category: Johansson P]] |
| - | [[Category: Koestler | + | [[Category: Koestler C]] |
| - | [[Category: Mulinacci | + | [[Category: Mulinacci B]] |
| - | [[Category: Oesterhelt | + | [[Category: Oesterhelt D]] |
| - | [[Category: Vollrath | + | [[Category: Vollrath R]] |
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Current revision
Saccharomyces cerevisiae FAS type I
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