| Structural highlights
4mrt is a 2 chain structure with sequence from Atcc 10027 and Bacsu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| Related: | 2md9, 1qr0, 2ge1 |
| Gene: | tycC (ATCC 10027), BSU03570, lpa-8, sfp (BACSU) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Function
[TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. [SFP_BACSU] Activates the seven peptidyl carrier protein (PCP) domains of surfactin synthase SRF1/2/3 by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for cells of B.subtilis to become producers of the lipopeptide antibiotics surfactin and plipastatin B1.[1]
Publication Abstract from PubMed
Phosphopantetheine transferases represent a class of enzymes found throughout all forms of life. From a structural point of view, they are subdivided into three groups, with transferases from group II being the most widespread. They are required for the posttranslational modification of carrier proteins involved in diverse metabolic pathways. We determined the crystal structure of the group II phosphopantetheine transferase Sfp from Bacillus in complex with a substrate carrier protein in the presence of coenzyme A and magnesium, and observed two protein-protein interaction sites. Mutational analysis showed that only the hydrophobic contacts between the carrier protein's second helix and the C-terminal domain of Sfp are essential for their productive interaction. Comparison with a similar structure of a complex of human proteins suggests that the mode of interaction is highly conserved in all domains of life.
Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification.,Tufar P, Rahighi S, Kraas FI, Kirchner DK, Lohr F, Henrich E, Kopke J, Dikic I, Guntert P, Marahiel MA, Dotsch V Chem Biol. 2014 Apr 2. pii: S1074-5521(14)00073-8. doi:, 10.1016/j.chembiol.2014.02.014. PMID:24704508[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel MA, Reid R, Khosla C, Walsh CT. A new enzyme superfamily - the phosphopantetheinyl transferases. Chem Biol. 1996 Nov;3(11):923-36. PMID:8939709
- ↑ Tufar P, Rahighi S, Kraas FI, Kirchner DK, Lohr F, Henrich E, Kopke J, Dikic I, Guntert P, Marahiel MA, Dotsch V. Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification. Chem Biol. 2014 Apr 2. pii: S1074-5521(14)00073-8. doi:, 10.1016/j.chembiol.2014.02.014. PMID:24704508 doi:http://dx.doi.org/10.1016/j.chembiol.2014.02.014
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