7zd3

Crystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase inhibited by Zn2+ ions

spinqualitylabelsall models 7zd3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zd3 is a 4 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: ADN, BCN, BU1, CL, HEZ, K, NAD, PDO, PG4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SAHH_PSEAE May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. Publication Abstract from PubMed We report biochemical and structural studies on inhibiting bacterial S-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. A closer look at molecular mechanisms underlying inhibition of S-adenosyl-L-homocysteine hydrolase by transition metal cations.,Gawel M, Malecki PH, Sliwiak J, Stepniewska M, Imiolczyk B, Czyrko-Horczak J, Jakubczyk D, Marczak L, Plonska-Brzezinska ME, Brzezinski K Chem Commun (Camb). 2024 Oct 8;60(81):11504-11507. doi: 10.1039/d4cc03143a. PMID:39230573 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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