2MD9

Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein

Summary for 2MD9

• Entry DOI: 10.2210/pdb2md9/pdb
• Related: 1DNY 2GDW 2GDX 2GDY 2GE1 4MRT
• NMR Information: BMRB: 19479
• Descriptor: Tyrocidine synthase 3 (1 entity in total)
• Functional Keywords: protein, carrier protein, ligase
• Biological source: Brevibacillus parabrevis
• Total number of polymer chains: 1
• Total formula weight: 9972.42

Authors

Tufar, P.,Rahighi, S.,Kraas, F.I.,Kirchner, D.K.,Loehr, F.,Henrich, E.,Koepke, J.,Dikic, I.,Guentert, P.,Marahiel, M.A.,Doetsch, V. (deposition date: 2013-09-06, release date: 2014-04-23, Last modification date: 2024-05-15)

Primary citation

Tufar, P.,Rahighi, S.,Kraas, F.I.,Kirchner, D.K.,Lohr, F.,Henrich, E.,Kopke, J.,Dikic, I.,Guntert, P.,Marahiel, M.A.,Dotsch, V.
Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification.
Chem.Biol., 21:552-562, 2014

PubMed Abstract: 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.

PubMed: 24704508
DOI: 10.1016/j.chembiol.2014.02.014

Experimental method

SOLUTION NMR