2fad: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2fad.gif|left|200px]]
{{Seed}}
[[Image:2fad.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fad|  PDB=2fad  |  SCENE=  }}  
{{STRUCTURE_2fad|  PDB=2fad  |  SCENE=  }}  


'''Crystal structure of E. coli heptanoyl-ACP'''
===Crystal structure of E. coli heptanoyl-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.
The line below this paragraph, {{ABSTRACT_PUBMED_17059829}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17059829 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17059829}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[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 Sun May  4 03:39:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:15:43 2008''

Revision as of 22:15, 27 July 2008

File:2fad.png

Template:STRUCTURE 2fad

Crystal structure of E. coli heptanoyl-ACP

Template:ABSTRACT PUBMED 17059829

About this Structure

2FAD 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

Page seeded by OCA on Mon Jul 28 01:15:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2fad&oldid=674940"