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PDBsum entry 1thm
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Hydrolase(serine protease)
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PDB id
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1thm
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References listed in PDB file
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Key reference
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Title
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Crystal structure of thermitase at 1.4 a resolution.
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Authors
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A.V.Teplyakov,
I.P.Kuranova,
E.H.Harutyunyan,
B.K.Vainshtein,
C.Frömmel,
W.E.Höhne,
K.S.Wilson.
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Ref.
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J Mol Biol, 1990,
214,
261-279.
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PubMed id
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Abstract
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The crystal structure of thermitase, a subtilisin-type serine proteinase from
Thermoactinomyces vulgaris, was determined by X-ray diffraction at 1.4 A
resolution. The structure was solved by a combination of molecular and
isomorphous replacement. The starting model was that of subtilisin BPN' from the
Protein Data Bank, determined at 2.5 A resolution. The high-resolution
refinement was based on data collected using synchrotron radiation with a Fuji
image plate as detector. The model of thermitase refined to a conventional R
factor of 14.9% and contains 1997 protein atoms, 182 water molecules and two Ca
ions. The tertiary structure of thermitase is similar to that of the other
subtilisins although there are some significant differences in detail.
Comparison with subtilisin BPN' revealed two major structural differences. The
N-terminal region in thermitase, which is absent in subtilisin BPN', forms a
number of contacts with the tight Ca2+ binding site and indeed provides the very
tight binding of the Ca ion. In thermitase the loop of residues 60 to 65 forms
an additional (10) beta-strand of the central beta-sheet and the second Ca2+
binding site that has no equivalent in the subtilisin BPN' structure. The
observed differences in the Ca2+ binding and the increased number of ionic and
aromatic interactions in thermitase are likely sources of the enhanced stability
of thermitase.
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Secondary reference #1
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Title
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Effects of eglin-C binding to thermitase: three-Dimensional structure comparison of native thermitase and thermitase eglin-C complexes.
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Authors
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P.Gros,
A.V.Teplyakov,
W.G.Hol.
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Ref.
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Proteins, 1992,
12,
63-74.
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PubMed id
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Secondary reference #2
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Title
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Thermitase and proteinase k: a comparison of the refined three-Dimensional structures of the native enzymes.
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Authors
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C.Betzel,
A.V.Teplyakov,
E.H.Harutyunyan,
W.Saenger,
K.S.Wilson.
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Ref.
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Protein Eng, 1990,
3,
161-172.
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PubMed id
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Secondary reference #3
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Title
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Crystal structure of thermitase from thermoactinomyces vulgaris at 2.2 a resolution.
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Authors
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A.V.Teplyakov,
I.P.Kuranova,
E.H.Harutyunyan,
C.Frömmel,
W.E.Höhne.
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Ref.
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Febs Lett, 1989,
244,
208-212.
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PubMed id
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Secondary reference #4
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Title
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X-Ray structural investigation of thermitase at a resolution of 2.5 angstroms
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Authors
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A.V.Teplyakov,
B.V.Strokopytov,
I.P.Kuranova,
A.N.Popov,
E.G.Arutyunyan,
B.K.Vainshtein,
K.Froemmel,
V.Khene.
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Ref.
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sov phys crystallogr (engl, 1987,
31,
553.
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Secondary reference #5
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Title
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Influence of calcium binding on the thermal stability of 'Thermitase', A serine protease from thermoactinomyces vulgaris.
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Authors
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C.Frömmel,
W.E.Höhne.
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Ref.
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Biochim Biophys Acta, 1981,
670,
25-31.
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PubMed id
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