1NX8

Structure of carbapenem synthase (CarC) complexed with N-acetyl proline

Summary for 1NX8

• Entry DOI: 10.2210/pdb1nx8/pdb
• Related: 1NX4
• Descriptor: Carbapenem synthase, FE (III) ION, 2-OXOGLUTARIC ACID, ... (5 entities in total)
• Functional Keywords: jelly roll, unknown function
• Biological source: Pectobacterium carotovorum
• Cellular location: Cytoplasm : Q9XB59
• Total number of polymer chains: 3
• Total formula weight: 95869.75

Authors

Clifton, I.J.,Doan, L.X.,Sleeman, M.C.,Topf, M.,Suzuki, H.,Wilmouth, R.C.,Schofield, C.J. (deposition date: 2003-02-10, release date: 2003-06-17, Last modification date: 2023-08-16)

Primary citation

Clifton, I.J.,Doan, L.X.,Sleeman, M.C.,Topf, M.,Suzuki, H.,Wilmouth, R.C.,Schofield, C.J.
Crystal structure of carbapenem synthase (CarC).
J.Biol.Chem., 278:20843-20850, 2003

PubMed Abstract: The proposed biosynthetic pathway to the carbapenem antibiotics proceeds via epimerization/desaturation of a carbapenam in an unusual process catalyzed by an iron- and 2-oxoglutarate-dependent oxygenase, CarC. Crystal structures of CarC complexed with Fe(II) and 2-oxoglutarate reveal it to be hexameric (space group C2221), consistent with solution studies. CarC monomers contain a double-stranded beta-helix core that supports ligands binding a single Fe(II) to which 2-oxoglutarate complexes in a bi-dentate manner. A structure was obtained with l-N-acetylproline acting as a substrate analogue. Quantum mechanical/molecular mechanical modeling studies with stereoisomers of carbapenams and carbapenems were used to investigate substrate binding. The combined work will stimulate further mechanistic studies and aid in the engineering of carbapenem biosynthesis.

PubMed: 12611886
DOI: 10.1074/jbc.M213054200

Experimental method

X-RAY DIFFRACTION (2.3 Å)