2uvc
From Proteopedia
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| - | [[Image:2uvc.gif|left|200px]]<br /> | + | [[Image:2uvc.gif|left|200px]]<br /><applet load="2uvc" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2uvc" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2uvc, resolution 3.1Å" /> | caption="2uvc, resolution 3.1Å" /> | ||
'''CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE COMPLEXED WITH NADP+ FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400'''<br /> | '''CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE COMPLEXED WITH NADP+ FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400'''<br /> | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2UVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus] with FMN and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2UVC with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. | + | 2UVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus] with FMN and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2UVC with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Known structural/functional Sites: <scene name='pdbsite=AC1:Fmn Binding Site For Chain G'>AC1</scene>, <scene name='pdbsite=AC2:Nap Binding Site For Chain G'>AC2</scene>, <scene name='pdbsite=AC3:Fmn Binding Site For Chain H'>AC3</scene>, <scene name='pdbsite=AC4:Nap Binding Site For Chain H'>AC4</scene>, <scene name='pdbsite=AC5:Fmn Binding Site For Chain I'>AC5</scene>, <scene name='pdbsite=AC6:Nap Binding Site For Chain I'>AC6</scene>, <scene name='pdbsite=AC7:Fmn Binding Site For Chain J'>AC7</scene>, <scene name='pdbsite=AC8:Nap Binding Site For Chain J'>AC8</scene>, <scene name='pdbsite=AC9:Fmn Binding Site For Chain K'>AC9</scene>, <scene name='pdbsite=BC1:Nap Binding Site For Chain K'>BC1</scene>, <scene name='pdbsite=BC2:Fmn Binding Site For Chain L'>BC2</scene> and <scene name='pdbsite=BC3:Nap Binding Site For Chain L'>BC3</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2UVC OCA]. |
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| + | ==Reference== | ||
| + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17431175 17431175] | ||
[[Category: Fatty Acid Synthase]] | [[Category: Fatty Acid Synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 20:16:59 2007'' |
Revision as of 18:07, 18 December 2007
|
CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE COMPLEXED WITH NADP+ FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400
Overview
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.
About this Structure
2UVC is a Single protein structure of sequence from Thermomyces lanuginosus with FMN and NAP as ligands. The following page contains interesting information on the relation of 2UVC with [Fatty Acid Synthase]. Known structural/functional Sites: , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Dec 18 20:16:59 2007
Categories: Fatty Acid Synthase | Single protein | Thermomyces lanuginosus | Ban, N. | Boehringer, D. | Frick, C. | Jenni, S. | Leibundgut, M. | Mikolasek, B. | FMN | NAP | Acetyl transferase | Acyl carrier protein | Dehydratase | Enoyl reductase | Fatty acid synthase | Fatty acid synthesis | Fungal | Ketoacyl reductase | Ketoacyl synthase | Malonyl/palmitoyl transferase | Multifunctional enzyme | Substrate shuttling | Transferase
