7KB0

O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine state

Summary for 7KB0

Entry DOI	10.2210/pdb7kb0/pdb
Descriptor	O-acetyl-L-homoserine sulfhydrylase (2 entities in total)
Functional Keywords	thermotoga maritima, methionine biosynthesis, enzyme kinetics, o-acety-l-homoserine aminocarboxypropyltransferase, mety, active site, transferase
Biological source	Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Total number of polymer chains	1
Total formula weight	47314.39
Authors	Brewster, J.L.,Pachl, P.,Squire, C.,Selmer, M.,Patrick, W.M. (deposition date: 2020-10-01, release date: 2021-06-23, Last modification date: 2024-04-03)
Primary citation	Brewster, J.L.,Pachl, P.,McKellar, J.L.O.,Selmer, M.,Squire, C.J.,Patrick, W.M. Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis. J.Biol.Chem., 296:100797-100797, 2021 Cited by PubMed: 34019879 DOI: 10.1016/j.jbc.2021.100797 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.85 Å)

Structure validation