2cdh: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cdh]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CDH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cdh]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CDH FirstGlance]. <br>
</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=2cdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cdh OCA], [https://pdbe.org/2cdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cdh RCSB], [https://www.ebi.ac.uk/pdbsum/2cdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cdh ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2&#8491;</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=2cdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cdh OCA], [https://pdbe.org/2cdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cdh RCSB], [https://www.ebi.ac.uk/pdbsum/2cdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cdh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABB_ECOLI FABB_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2cdh ConSurf].
</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=2cdh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha6beta6 complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual steps of the reaction pathway into a 5 angstrom x-ray crystallographic electron density map. The huge assembly contains two separated reaction chambers, each equipped with three sets of active sites separated by distances up to approximately 130 angstroms, across which acyl carrier protein shuttles substrates during the reaction cycle. Regions of the electron density arising from well-defined structural features outside the catalytic domains separate the two reaction chambers and serve as a matrix in which domains carrying the various active sites are embedded. The structure rationalizes the compartmentalization of fatty acid synthesis, and the spatial arrangement of the active sites has specific implications for our understanding of the reaction cycle mechanism and of the architecture of multienzymes in general.
Architecture of a fungal fatty acid synthase at 5 A resolution.,Jenni S, Leibundgut M, Maier T, Ban N Science. 2006 Mar 3;311(5765):1263-7. PMID:16513976<ref>PMID:16513976</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cdh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thermomyces lanuginosus]]
[[Category: Thermomyces lanuginosus]]
[[Category: Ban, N]]
[[Category: Ban N]]
[[Category: Jenni, S]]
[[Category: Jenni S]]
[[Category: Leibundgut, M]]
[[Category: Leibundgut M]]
[[Category: Maier, T]]
[[Category: Maier T]]
[[Category: Fatty acid synthesis]]
[[Category: Fungal fatty acid synthase]]
[[Category: Multifunctional enzyme]]
[[Category: Transferase]]

Latest revision as of 09:17, 14 February 2024

ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.

2cdh, resolution 4.20Å

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