1fth

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CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (3'5'-ADP COMPLEX)CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (3'5'-ADP COMPLEX)

Structural highlights

1fth is a 3 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACPS_STRPN Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein (By similarity).[HAMAP-Rule:MF_00101]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Acyl carrier protein synthase (AcpS) catalyzes the formation of holo-ACP, which mediates the essential transfer of acyl fatty acid intermediates during the biosynthesis of fatty acids and lipids in the cell. Thus, AcpS plays an important role in bacterial fatty acid and lipid biosynthesis, making it an attractive target for therapeutic intervention. We have determined, for the first time, the crystal structure of the Streptococcus pneumoniae AcpS and AcpS complexed with 3'5'-ADP, a product of AcpS, at 2.0 and 1.9 A resolution, respectively. The crystal structure reveals an alpha/beta fold and shows that AcpS assembles as a tightly packed functional trimer, with a non-crystallographic pseudo-symmetric 3-fold axis, which contains three active sites at the interface between protomers. Only two active sites are occupied by the ligand molecules. Although there is virtually no sequence similarity between the S.pneumoniae AcpS and the Bacillus subtilis Sfp transferase, a striking structural similarity between both enzymes was observed. These data provide a starting point for structure-based drug design efforts towards the identification of AcpS inhibitors with potent antibacterial activity.

Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis.,Chirgadze NY, Briggs SL, McAllister KA, Fischl AS, Zhao G EMBO J. 2000 Oct 16;19(20):5281-7. PMID:11032795[1]

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

See Also

References

  1. Chirgadze NY, Briggs SL, McAllister KA, Fischl AS, Zhao G. Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis. EMBO J. 2000 Oct 16;19(20):5281-7. PMID:11032795 doi:http://dx.doi.org/10.1093/emboj/19.20.5281

1fth, resolution 1.90Å

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