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PDBsum entry 1ba1
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References listed in PDB file
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Key reference
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Title
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Structural replacement of active site monovalent cations by the epsilon-Amino group of lysine in the atpase fragment of bovine hsc70.
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Authors
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S.M.Wilbanks,
D.B.Mckay.
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Ref.
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Biochemistry, 1998,
37,
7456-7462.
[DOI no: ]
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PubMed id
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Abstract
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We have assessed the ability of the epsilon-amino group of a non-native lysine
chain to substitute for a monovalent cation in an enzyme active site. In the
bovine Hsc70 ATPase fragment, mutation of cysteine 17 or aspartic acid 206 to
lysine potentially allows the replacement of an active site potassium ion with
the epsilon-amino nitrogen. We examined the ATP hydrolysis kinetics and crystal
structures of isolated mutant ATPase domains. The introduced epsilon-amino
nitrogen in the C17K mutant occupies a significantly different position than the
potassium ion. The introduced epsilon-amino nitrogen in the D206K mutant
occupies a position indistinguishable from that of the potassium in the
wild-type structure. Each mutant retains <5% ATPase activity when compared to
the wild type under physiological conditions (potassium buffer) although
substrate binding is tighter, probably as a consequence of slower release. It is
possible to construct a very good structural mimic of bound cation which
suffices for substrate binding but not for catalytic activity.
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Secondary reference #1
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Title
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Structural basis of the 70-Kilodalton heat shock cognate protein ATP hydrolytic activity. Ii. Structure of the active site with ADP or ATP bound to wild type and mutant atpase fragment.
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Authors
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K.M.Flaherty,
S.M.Wilbanks,
C.Deluca-Flaherty,
D.B.Mckay.
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Ref.
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J Biol Chem, 1994,
269,
12899-12907.
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PubMed id
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Secondary reference #2
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Title
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Three-Dimensional structure of the atpase fragment of a 70k heat-Shock cognate protein.
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Authors
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K.M.Flaherty,
C.Deluca-Flaherty,
D.B.Mckay.
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Ref.
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Nature, 1990,
346,
623-628.
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PubMed id
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