1a7a
From Proteopedia
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STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hypermethioninemia with deficiency of S-adenosylhomocysteine hydrolase OMIM:[180960]
About this Structure
1A7A is a Single protein structure of sequence from Homo sapiens with NAD and ADC as ligands. Active as Adenosylhomocysteinase, with EC number 3.3.1.1 Full crystallographic information is available from OCA.
Reference
Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength., Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, Howell PL, Nat Struct Biol. 1998 May;5(5):369-76. PMID:9586999
Page seeded by OCA on Mon Nov 12 15:56:21 2007
