2uvc
From Proteopedia
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|PDB= 2uvc |SIZE=350|CAPTION= <scene name='initialview01'>2uvc</scene>, resolution 3.1Å | |PDB= 2uvc |SIZE=350|CAPTION= <scene name='initialview01'>2uvc</scene>, resolution 3.1Å | ||
|SITE= <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> | |SITE= <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> | ||
| - | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2uvb|2UVB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uvc OCA], [http://www.ebi.ac.uk/pdbsum/2uvc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uvc RCSB]</span> | ||
}} | }} | ||
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[[Category: Leibundgut, M.]] | [[Category: Leibundgut, M.]] | ||
[[Category: Mikolasek, B.]] | [[Category: Mikolasek, B.]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: NAP]] | ||
[[Category: acetyl transferase]] | [[Category: acetyl transferase]] | ||
[[Category: acyl carrier protein]] | [[Category: acyl carrier protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:05:02 2008'' |
Revision as of 02:05, 31 March 2008
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| , resolution 3.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , and | ||||||
| Ligands: | , | ||||||
| Related: | 2UVB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. The following page contains interesting information on the relation of 2UVC with [Fatty Acid Synthase]. 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 Mon Mar 31 05:05:02 2008
Categories: Fatty Acid Synthase | Single protein | Thermomyces lanuginosus | Ban, N. | Boehringer, D. | Frick, C. | Jenni, S. | Leibundgut, M. | Mikolasek, B. | 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
