1fte: Difference between revisions
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[[Image:1fte.gif|left|200px]] | [[Image:1fte.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (NATIVE 1)''' | {{Structure | ||
|PDB= 1fte |SIZE=350|CAPTION= <scene name='initialview01'>1fte</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Holo-[acyl-carrier-protein]_synthase Holo-[acyl-carrier-protein] synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.7 2.7.8.7] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (NATIVE 1)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FTE is a [ | 1FTE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTE OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11032795 11032795] | ||
[[Category: Holo-[acyl-carrier-protein] synthase]] | [[Category: Holo-[acyl-carrier-protein] synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:13:45 2008'' | ||
Revision as of 12:13, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Activity: | [acyl-carrier-protein_synthase Holo-[acyl-carrier-protein] synthase], with EC number 2.7.8.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (NATIVE 1)
OverviewOverview
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.
About this StructureAbout this Structure
1FTE is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
ReferenceReference
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 [[Category: Holo-[acyl-carrier-protein] synthase]]
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