2PYW

Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR

Summary for 2PYW

Entry DOI	10.2210/pdb2pyw/pdb
Descriptor	Uncharacterized protein, CHLORIDE ION, MAGNESIUM ION, ... (7 entities in total)
Functional Keywords	5-methylthioribose kinase, plant methionine recycling, refolding, transferase
Biological source	Arabidopsis thaliana (thale cress)
Total number of polymer chains	2
Total formula weight	97978.95
Authors	Ku, S.Y. (deposition date: 2007-05-16, release date: 2008-01-15, Last modification date: 2023-08-30)
Primary citation	Ku, S.Y.,Cornell, K.A.,Howell, P.L. Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR reveals a more occluded active site than its bacterial homolog Bmc Struct.Biol., 7:70-70, 2007 Cited by PubMed Abstract: Metabolic variations exist between the methionine salvage pathway of humans and a number of plants and microbial pathogens. 5-Methylthioribose (MTR) kinase is a key enzyme required for methionine salvage in plants and many bacteria. The absence of a mammalian homolog suggests that MTR kinase is a good target for the design of specific herbicides or antibiotics. PubMed: 17961230 DOI: 10.1186/1472-6807-7-70 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation