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PDBsum entry 1ypi
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Isomerase(intramolecular oxidoreductase)
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PDB id
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1ypi
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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 of yeast triosephosphate isomerase at 1.9-A resolution.
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Authors
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E.Lolis,
T.Alber,
R.C.Davenport,
D.Rose,
F.C.Hartman,
G.A.Petsko.
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Ref.
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Biochemistry, 1990,
29,
6609-6618.
[DOI no: ]
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PubMed id
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Abstract
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The structure of yeast triosephosphate isomerase (TIM) has been solved at 3.0-A
resolution and refined at 1.9-A resolution to an R factor of 21.0%. The final
model consists of all non-hydrogen atoms in the polypeptide chain and 119 water
molecules, a number of which are found in the interior of the protein. The
structure of the active site clearly indicates that the carboxylate of the
catalytic base, Glu 165, is involved in a hydrogen-bonding interaction with the
hydroxyl of Ser 96. In addition, the interactions of the other active site
residues, Lys 12 and His 95, are also discussed. For the first time in any TIM
structure, the "flexible loop" has well-defined density; the conformation of the
loop in this structure is stabilized by a crystal contact. Analysis of the
subunit interface of this dimeric enzyme hints at the source of the specificity
of one subunit for another and allows us to estimate an association constant of
10(14)-10(16) M-1 for the two monomers. The analysis also suggests that the
interface may be a particularly good target for drug design. The conserved
positions (20%) among sequences from 13 sources ranging on the evolutionary
scale from Escherichia coli to humans reveal the intense pressure to maintain
the active site structure.
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Secondary reference #1
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Title
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Crystallographic analysis of the complex between triosephosphate isomerase and 2-Phosphoglycolate at 2.5-A resolution: implications for catalysis.
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Authors
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E.Lolis,
G.A.Petsko.
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Ref.
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Biochemistry, 1990,
29,
6619-6625.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Crystallography and site-Directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
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Authors
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T.C.Alber,
R.C.Davenport,
D.A.Giammona,
E.Lolis,
G.A.Petsko,
D.Ringe.
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Ref.
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Cold Spring Harb Symp Quant Biol, 1987,
52,
603-613.
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PubMed id
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Secondary reference #3
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Title
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Crystallization of yeast triose phosphate isomerase from polyethylene glycol. Protein crystal formation following phase separation.
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Authors
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T.Alber,
F.C.Hartman,
R.M.Johnson,
G.A.Petsko,
D.Tsernoglou.
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Ref.
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J Biol Chem, 1981,
256,
1356-1361.
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PubMed id
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Secondary reference #4
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Title
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On the three-Dimensional structure and catalytic mechanism of triose phosphate isomerase.
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Authors
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T.Alber,
D.W.Banner,
A.C.Bloomer,
G.A.Petsko,
D.Phillips,
P.S.Rivers,
I.A.Wilson.
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Ref.
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Philos Trans R Soc Lond B Biol Sci, 1981,
293,
159-171.
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PubMed id
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