7ZD4

Crystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ions

Summary for 7ZD4

Entry DOI	10.2210/pdb7zd4/pdb
Descriptor	Adenosylhomocysteinase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ADENOSINE, ... (7 entities in total)
Functional Keywords	regulation of sam-dependent methylation reactions, inhibition, metal binding, copper, disulfide bond, hydrolase
Biological source	Pseudomonas aeruginosa PAO1
Total number of polymer chains	4
Total formula weight	211371.78
Authors	Malecki, P.H.,Gawel, M.,Brzezinski, K. (deposition date: 2022-03-29, release date: 2023-04-19, Last modification date: 2024-10-30)
Primary citation	Gawel, M.,Malecki, P.H.,Sliwiak, J.,Stepniewska, M.,Imiolczyk, B.,Czyrko-Horczak, J.,Jakubczyk, D.,Marczak, L.,Plonska-Brzezinska, M.E.,Brzezinski, K. A closer look at molecular mechanisms underlying inhibition of S -adenosyl-L-homocysteine hydrolase by transition metal cations. Chem.Commun.(Camb.), 60:11504-11507, 2024 Cited by PubMed Abstract: We report biochemical and structural studies on inhibiting bacterial -adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor. PubMed: 39230573 DOI: 10.1039/d4cc03143a PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.14 Å)

Structure validation