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1qr0
From Proteopedia
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|PDB= 1qr0 |SIZE=350|CAPTION= <scene name='initialview01'>1qr0</scene>, resolution 1.90Å | |PDB= 1qr0 |SIZE=350|CAPTION= <scene name='initialview01'>1qr0</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= SFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qr0 OCA], [http://www.ebi.ac.uk/pdbsum/1qr0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qr0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Mofid, R M.]] | [[Category: Mofid, R M.]] | ||
[[Category: Reuter, K.]] | [[Category: Reuter, K.]] | ||
| - | [[Category: COA]] | ||
| - | [[Category: MG]] | ||
[[Category: protein-coenzyme a complex]] | [[Category: protein-coenzyme a complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:44 2008'' |
Revision as of 20:17, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SFP (Bacillus subtilis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE 4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP-COENZYME A COMPLEX
Overview
The Bacillus subtilis Sfp protein activates the peptidyl carrier protein (PCP) domains of surfactin synthetase by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue conserved in all PCPs. Its wide PCP substrate spectrum renders Sfp a biotechnologically valuable enzyme for use in combinatorial non-ribosomal peptide synthesis. The structure of the Sfp-CoA complex determined at 1.8 A resolution reveals a novel alpha/beta-fold exhibiting an unexpected intramolecular 2-fold pseudosymmetry. This suggests a similar fold and dimerization mode for the homodimeric phosphopantetheinyl transferases such as acyl carrier protein synthase. The active site of Sfp accommodates a magnesium ion, which is complexed by the CoA pyrophosphate, the side chains of three acidic amino acids and one water molecule. CoA is bound in a fashion that differs in many aspects from all known CoA-protein complex structures. The structure reveals regions likely to be involved in the interaction with the PCP substrate.
About this Structure
1QR0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily., Reuter K, Mofid MR, Marahiel MA, Ficner R, EMBO J. 1999 Dec 1;18(23):6823-31. PMID:10581256
Page seeded by OCA on Sun Mar 30 23:17:44 2008
