4HZN

The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double Hot Dog Fold

Summary for 4HZN

Entry DOI	10.2210/pdb4hzn/pdb
Related	4HZO 4HZP
Descriptor	Bifunctional Methylmalonyl-CoA:ACP Acyltransferase/Decarboxylase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, GLYCEROL, ... (5 entities in total)
Functional Keywords	structural genomics, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, psi-biology, double hot dog fold, bifunctional methylmalonyl-coa:acp acyltransferase/decarboxylase, acyl carrier protein (lnmk) methylmalonyl-coa, transferase
Biological source	Streptomyces atroolivaceus
Total number of polymer chains	1
Total formula weight	38073.36
Authors	Lohman, J.R.,Bingman, C.A.,Phillips Jr., G.N.,Shen, B.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2012-11-15, release date: 2013-01-30, Last modification date: 2013-02-20)
Primary citation	Lohman, J.R.,Bingman, C.A.,Phillips, G.N.,Shen, B. Structure of the Bifunctional Acyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double-Hot-Dog Fold. Biochemistry, 52:902-911, 2013 Cited by PubMed: 23320975 DOI: 10.1021/bi301652y PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.25 Å)

Structure validation