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PDBsum entry 1mlv
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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 and catalytic mechanism of a set domain protein methyltransferase.
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Authors
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R.C.Trievel,
B.M.Beach,
L.M.Dirk,
R.L.Houtz,
J.H.Hurley.
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Ref.
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Cell, 2002,
111,
91.
[DOI no: ]
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PubMed id
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Abstract
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Protein lysine methylation by SET domain enzymes regulates chromatin structure,
gene silencing, transcriptional activation, plant metabolism, and other
processes. The 2.6 A resolution structure of Rubisco large subunit
methyltransferase in a pseudo-bisubstrate complex with S-adenosylhomocysteine
and a HEPES ion reveals an all-beta architecture for the SET domain embedded
within a larger alpha-helical enzyme fold. Conserved regions of the SET domain
bind S-adenosylmethionine and substrate lysine at two sites connected by a pore.
We propose that methyl transfer is catalyzed by a conserved Tyr at a narrow pore
connecting the sites. The cofactor enters by a "back door" on the
opposite side of the enzyme from substrate, promoting highly specific protein
recognition and allowing addition of multiple methyl groups.
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Figure 1.
Figure 1. Structure of LSMT and the SET Domain
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Figure 4.
Figure 4. Ligand Binding Sites
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2002,
111,
91-0)
copyright 2002.
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