2fae: Difference between revisions
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|PDB= 2fae |SIZE=350|CAPTION= <scene name='initialview01'>2fae</scene>, resolution 1.550Å | |PDB= 2fae |SIZE=350|CAPTION= <scene name='initialview01'>2fae</scene>, resolution 1.550Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=PM8:S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL)+DECANETHIOATE'>PM8</scene>, <scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1l0h|1L0H]], [[1l0i|1L0I]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fae OCA], [http://www.ebi.ac.uk/pdbsum/2fae PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fae RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Roujeinikova, A.]] | [[Category: Roujeinikova, A.]] | ||
[[Category: acyl carrier protein]] | [[Category: acyl carrier protein]] | ||
[[Category: acyl chain binding]] | [[Category: acyl chain binding]] | ||
[[Category: fatty acid biosynthesis]] | [[Category: fatty acid biosynthesis]] | ||
''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 03:00:07 2008'' | ||
Revision as of 03:00, 31 March 2008
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| , resolution 1.550Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1L0H, 1L0I
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of E. coli decanoyl-ACP
OverviewOverview
A knowledge of the structures of acyl chain loaded species of the acyl carrier protein (ACP) as used in fatty acid biosynthesis and a range of other metabolic events, is essential for a full understanding of the molecular recognition at the heart of these processes. To date the only crystal structure of an acylated species of ACP is that of a butyryl derivative of Escherichia coli ACP. We have now determined the structures of a family of acylated E. coli ACPs of varying acyl chain length. The acyl moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a serine residue in ACP. The growing acyl chain can be accommodated within a central cavity in the ACP for transport during the elongation stages of lipid synthesis through changes in the conformation of a four alpha-helix bundle. The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.
About this StructureAbout this Structure
2FAE is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 2FAE with [Fatty Acid Synthase]. Full crystallographic information is available from OCA.
ReferenceReference
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates., Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR, J Mol Biol. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:17059829
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