View source for 2fac

[[Image:2fac.gif|left|200px]]

 {{Structure
|PDB= 2fac |SIZE=350|CAPTION= <scene name='initialview01'>2fac</scene>, resolution 1.760&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=PM4:S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL)+HEXANETHIOATE'>PM4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY= 
|GENE= acpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|DOMAIN=
|RELATEDENTRY=[[1l0h|1L0H]], [[1l0i|1L0I]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fac OCA], [http://www.ebi.ac.uk/pdbsum/2fac PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fac RCSB]</span>
}}

'''Crystal structure of E. coli hexanoyl-ACP'''


==Overview==
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 Structure==
2FAC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAC OCA]. 

==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17059829 17059829]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Roujeinikova, A.]]
[[Category: acyl carrier protein]]
[[Category: acyl chain binding]]
[[Category: fatty acid biosynthesis]]

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