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2fac

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[[Image:2fac.gif|left|200px]]<br /><applet load="2fac" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fac.gif|left|200px]]
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caption="2fac, resolution 1.760&Aring;" />
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'''Crystal structure of E. coli hexanoyl-ACP'''<br />
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{{Structure
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|PDB= 2fac |SIZE=350|CAPTION= <scene name='initialview01'>2fac</scene>, resolution 1.760&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PM4:S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEXANETHIOATE'>PM4</scene>
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|ACTIVITY=
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|GENE= acpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of E. coli hexanoyl-ACP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PM4:'>PM4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAC OCA].
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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==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17059829 17059829]
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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: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: fatty acid biosynthesis]]
[[Category: fatty acid biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:50:00 2008''

Revision as of 14:50, 20 March 2008


PDB ID 2fac

Drag the structure with the mouse to rotate
, resolution 1.760Å
Ligands: and
Gene: acpP (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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 Escherichia coli. Full crystallographic information is available from 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:17059829

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