View source for 4v58


==Crystal structure of fatty acid synthase from thermomyces lanuginosus at 3.1 angstrom resolution.==
<StructureSection load='4v58' size='340' side='right'caption='[[4v58]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4v58]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2uv9 2uv9] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2uva 2uva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V58 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]] 3.1&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=4v58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v58 OCA], [https://pdbe.org/4v58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v58 RCSB], [https://www.ebi.ac.uk/pdbsum/4v58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v58 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.

Structure of fungal fatty acid synthase and implications for iterative substrate shuttling.,Jenni S, Leibundgut M, Boehringer D, Frick C, Mikolasek B, Ban N Science. 2007 Apr 13;316(5822):254-61. PMID:17431175<ref>PMID:17431175</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4v58" 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: Thermomyces lanuginosus]]
[[Category: Ban N]]
[[Category: Boehringer D]]
[[Category: Frick C]]
[[Category: Jenni S]]
[[Category: Leibundgut M]]
[[Category: Mikolasek B]]