2CG5

Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with cytosolic acyl carrier protein and coenzyme A

Summary for 2CG5

• Entry DOI: 10.2210/pdb2cg5/pdb
• Related: 2BYD 2C43
• Descriptor: L-AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE, FATTY ACID SYNTHASE, COENZYME A, ... (7 entities in total)
• Functional Keywords: transferase-hydrolase complex, transferase-hydrolase (complex), fatty acid biosynthesis, phosphopantetheine transferase, fasn, acp, coenzyme a, transferase, hydrolase, lipid synthesis, lyase, complex, transferase/hydrolase
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm : Q9NRN7 P49327
• Total number of polymer chains: 2
• Total formula weight: 48087.11

Authors

Bunkoczi, G.,Joshi, A.,Papagrigoriu, E.,Arrowsmith, C.,Edwards, A.,Sundstrom, M.,Weigelt, J.,von Delft, F.,Smith, S.,Oppermann, U. (deposition date: 2006-02-27, release date: 2006-03-01, Last modification date: 2023-12-13)

Primary citation

Bunkoczi, G.,Pasta, S.,Joshi, A.,Wu, X.,Kavanagh, K.L.,Smith, S.,Oppermann, U.
Mechanism and Substrate Recognition of Human Holo Acp Synthase.
Chem.Biol., 14:1243-, 2007

PubMed Abstract: Mammals utilize a single phosphopantetheinyl transferase for the posttranslational modification of at least three different apoproteins: the carrier protein components of cytosolic and mitochondrial fatty acid synthases and the aminoadipate semialdehyde reductase involved in lysine degradation. We determined the crystal structure of the human phosphopantetheinyl transferase, a eukaryotic phosphopantetheinyl transferase characterized, complexed with CoA and Mg(2+), and in ternary complex with CoA and ACP. The involvement of key residues in ligand binding and catalysis was confirmed by mutagenesis and kinetic analysis. Human phosphopantetheinyl transferase exhibits an alpha/beta fold and 2-fold pseudosymmetry similar to the Sfp phosphopantetheinyl transferase from Bacillus subtilis. Although the bound ACP exhibits a typical four-helix structure, its binding is unusual in that it is facilitated predominantly by hydrophobic interactions. A detailed mechanism is proposed describing the substrate binding and catalytic process.

PubMed: 18022563
DOI: 10.1016/J.CHEMBIOL.2007.10.013

Experimental method

X-RAY DIFFRACTION (2.7 Å)