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| - | [[Image:1f7l.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1f7l| PDB=1f7l | SCENE= }} | | {{STRUCTURE_1f7l| PDB=1f7l | SCENE= }} |
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| - | '''HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A'''
| + | ===HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A=== |
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| - | ==Overview==
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| - | BACKGROUND: Holo-(acyl carrier protein) synthase (AcpS), a member of the phosphopantetheinyl transferase superfamily, plays a crucial role in the functional activation of acyl carrier protein (ACP) in the fatty acid biosynthesis pathway. AcpS catalyzes the attachment of the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to the sidechain of a conserved serine residue on apo-ACP. RESULTS: We describe here the first crystal structure of a type II ACP from Bacillus subtilis in complex with its activator AcpS at 2.3 A. We also have determined the structures of AcpS alone (at 1.8 A) and AcpS in complex with CoA (at 1.5 A). These structures reveal that AcpS exists as a trimer. A catalytic center is located at each of the solvent-exposed interfaces between AcpS molecules. Site-directed mutagenesis studies confirm the importance of trimer formation in AcpS activity. CONCLUSIONS: The active site in AcpS is only formed when two AcpS molecules dimerize. The addition of a third molecule allows for the formation of two additional active sites and also permits a large hydrophobic surface from each molecule of AcpS to be buried in the trimer. The mutations Ile5-->Arg, Gln113-->Glu and Gln113-->Arg show that AcpS is inactive when unable to form a trimer. The co-crystal structures of AcpS-CoA and AcpS-ACP allow us to propose a catalytic mechanism for this class of 4'-phosphopantetheinyl transferases.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10997907}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10997907 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10997907}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tam, A.]] | | [[Category: Tam, A.]] |
| | [[Category: 9-strand pseudo beta barrel protein,coa complex protein,coenzyme a complex]] | | [[Category: 9-strand pseudo beta barrel protein,coa complex protein,coenzyme a complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:59:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:49:41 2008'' |
Revision as of 23:49, 30 June 2008
Template:STRUCTURE 1f7l
HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A
Template:ABSTRACT PUBMED 10997907
About this Structure
1F7L is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites., Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS, Structure. 2000 Aug 15;8(8):883-95. PMID:10997907
Page seeded by OCA on Tue Jul 1 02:49:41 2008
Categories: Bacillus subtilis | Single protein | Fritz, C C. | Hixon, J. | Lin, L. | Mathew, R. | Parris, K D. | Seehra, J. | Somers, W S. | Stahl, M. | Tam, A. | 9-strand pseudo beta barrel protein,coa complex protein,coenzyme a complex
