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PDBsum entry 1a7a
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure determination of selenomethionyl s-Adenosylhomocysteine hydrolase using data at a single wavelength.
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Authors
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M.A.Turner,
C.S.Yuan,
R.T.Borchardt,
M.S.Hershfield,
G.D.Smith,
P.L.Howell.
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Ref.
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Nat Struct Biol, 1998,
5,
369-376.
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PubMed id
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Abstract
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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.
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