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1f80

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1f80, resolution 2.30Å ()
Ligands:
Non-Standard Residues:
Activity: [acyl-carrier-protein_synthase Holo-[acyl-carrier-protein] synthase], with EC number 2.7.8.7
Domains: acpS, acpP
Related: 1f7t, 1f7l
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH HOLO-(ACYL CARRIER PROTEIN)

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

The B. subtilis AcpS trimer (1f80) three molecules of the acyl carrier protein (ASP). The interactions between B. subtilis AcpS and ACP are predominantly . The B. subtilis AcpS (white) is shown in spacefill representation, the agrinines, lysines, and histidines are colored blue, while aspartates and glutamates are colored red. The ACP molecule (lime) is shown in ribbon representation with aspartates and glutamates as sticks and colored red. The B. subtilis AcpS has large with ASP. of Mycobacterium tuberculosis (Mtb) AcpS (3hqj) surface using the similar orientation as B. subtilis AcpS, shows a moderate electronegative nature in the putative ACP binding site near the ASP 15. The Mtb ASPM structure (1klp, corresponding to ACP) demonstrates considerably lower negative charge. So, the electrostatic interactions between Mtb AcpS and ASPM are, probably, less important.

About this Structure

1F80 is a 6 chains structure of sequences from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

  • Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS. 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. Structure. 2000 Aug 15;8(8):883-95. PMID:10997907
  • Dym O, Albeck S, Peleg Y, Schwarz A, Shakked Z, Burstein Y, Zimhony O. Structure-function analysis of the acyl carrier protein synthase (AcpS) from Mycobacterium tuberculosis. J Mol Biol. 2009 Nov 6;393(4):937-50. Epub 2009 Sep 3. PMID:19733180 doi:10.1016/j.jmb.2009.08.065

Page seeded by OCA on Mon Feb 16 23:04:18 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA, Alexander Berchansky

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