5DDS

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PLP

Summary for 5DDS

• Entry DOI: 10.2210/pdb5dds/pdb
• Related: 5DDU 5DDW
• Descriptor: CrmG, PYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: aminotransferase, plp, caerulomycin a, transferase
• Biological source: Actinoalloteichus sp. WH1-2216-6
• Total number of polymer chains: 4
• Total formula weight: 230110.89

Authors

Xu, J.,Feng, Z.,Liu, J. (deposition date: 2015-08-25, release date: 2016-08-10)

Primary citation

Zhu, Y.,Xu, J.,Mei, X.,Feng, Z.,Zhang, L.,Zhang, Q.,Zhang, G.,Zhu, W.,Liu, J.,Zhang, C.
Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis
Acs Chem.Biol., 11:943-952, 2016

PubMed Abstract: Caerulomycin A (CRM A 1) belongs to a family of natural products containing a 2,2'-bipyridyl ring core structure and is currently under development as a potent novel immunosuppressive agent. Herein, we report the functional characterization, kinetic analysis, substrate specificity, and structure insights of an aminotransferase CrmG in 1 biosynthesis. The aminotransferase CrmG was confirmed to catalyze a key transamination reaction to convert an aldehyde group to an amino group in the 1 biosynthetic pathway, preferring l-glutamate and l-glutamine as the amino donor substrates. The crystal structures of CrmG in complex with the cofactor 5'-pyridoxal phosphate (PLP) or 5'-pyridoxamine phosphate (PMP) or the acceptor substrate were determined to adopt a canonical fold-type I of PLP-dependent enzymes with a unique small additional domain. The structure guided site-directed mutagenesis identified key amino acid residues for substrate binding and catalytic activities, thus providing insights into the transamination mechanism of CrmG.

PubMed: 26714051
DOI: 10.1021/acschembio.5b00984

Experimental method

X-RAY DIFFRACTION (2.6 Å)