1A7A

STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH

Summary for 1A7A

• Entry DOI: 10.2210/pdb1a7a/pdb
• Descriptor: S-ADENOSYLHOMOCYSTEINE HYDROLASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, (1'R,2'S)-9-(2-HYDROXY-3'-KETO-CYCLOPENTEN-1-YL)ADENINE, ... (4 entities in total)
• Functional Keywords: hydrolase, nad binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P23526
• Total number of polymer chains: 2
• Total formula weight: 98837.87

Authors

Turner, M.A.,Yuan, C.-S.,Borchardt, R.T.,Hershfield, M.S.,Smith, G.D.,Howell, P.L. (deposition date: 1998-03-10, release date: 1999-04-20, Last modification date: 2024-10-23)

Primary citation

Turner, M.A.,Yuan, C.S.,Borchardt, R.T.,Hershfield, M.S.,Smith, G.D.,Howell, P.L.
Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength.
Nat.Struct.Biol., 5:369-376, 1998

PubMed Abstract: S-Adenosylhomocysteine (AdoHcy) hydrolase regulates all adenosylmethionine-(AdoMet) dependent transmethylations by hydrolyzing the potent feedback inhibitor AdoHcy to homocysteine and adenosine. The crystallographic structure determination of a selenomethionyl-incorporated AdoHcy hydrolase inhibitor complex was accomplished using single wavelength anomalous diffraction data and the direct methods program, Snb v2.0, which produced the positions of all 30 crystallographically distinct selenium atoms. The mode of enzyme-cofactor binding is unique, requiring interactions from two protein monomers. An unusual dual role for a catalytic water molecule in the active site is revealed in the complex with the adenosine analog 2'-hydroxy, 3'-ketocyclopent-4'-enyladenine.

PubMed: 9586999
DOI: 10.1038/nsb0598-369

Experimental method

X-RAY DIFFRACTION (2.8 Å)