4mrt | pdb_00004mrt

Structure of the Phosphopantetheine Transferase Sfp in Complex with Coenzyme A and a Peptidyl Carrier Protein

spinqualitylabelsall models 4mrt, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mrt is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168 and Brevibacillus parabrevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: COA, GOL, MG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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