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PDBsum entry 2tbs
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Hydrolase(serine proteinase)
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PDB id
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2tbs
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References listed in PDB file
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Key reference
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Title
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Cold adaption of enzymes: structural comparison between salmon and bovine trypsins.
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Authors
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A.O.Smalås,
E.S.Heimstad,
A.Hordvik,
N.P.Willassen,
R.Male.
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Ref.
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Proteins, 1994,
20,
149-166.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above were
obtained from the PDBe's
server.
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Abstract
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The crystal structure of an anionic form of salmon trypsin has been determined
at 1.82 A resolution. We report the first structure of a trypsin from a
phoikilothermic organism in a detailed comparison to mammalian trypsins in order
to look for structural rationalizations for the cold-adaption features of salmon
trypsin. This form of salmon trypsin (ST II) comprises 222 residues, and is
homologous to bovine trypsin (BT) in about 65% of the primary structure. The
tertiary structures are similar, with an overall displacement in main chain
atomic positions between salmon trypsin and various crystal structures of bovine
trypsin of about 0.8 A. Intramolecular hydrogen bonds and hydrophobic
interactions are compared and discussed in order to estimate possible
differences in molecular flexibility which might explain the higher catalytic
efficiency and lower thermostability of salmon trypsin compared to bovine
trypsin. No overall differences in intramolecular interactions are detected
between the two structures, but there are differences in certain regions of the
structures which may explain some of the observed differences in physical
properties. The distribution of charged residues is different in the two
trypsins, and the impact this might have on substrate affinity has been
discussed.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray crystallographic studies of benzamidine-Inhibited trypsin from the north atlantic salmon (salmo salar).
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Authors
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A.O.Smalås,
A.Hordvik,
L.K.Hansen,
E.Hough,
K.Jynge.
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Ref.
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J Mol Biol, 1990,
214,
355-358.
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PubMed id
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Secondary reference #2
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Title
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Crystallization and preliminary X-Ray crystallographic studies of benzamidine-Inhibited trypsin from the north atlantic salmon (salmo salar).
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Authors
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A.O.Smalås,
A.Hordvik,
L.K.Hansen,
E.Hough,
K.Jynge.
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Ref.
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J Mol Biol, 1990,
214,
355-358.
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PubMed id
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Secondary reference #3
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Title
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The geometry of the reactive site and of the peptide groups in trypsin, Trypsinogen and its complexes with inhibitors
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Authors
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M.Marquart,
J.Walter,
J.Deisenhofer,
W.Bode,
R.Huber.
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Ref.
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acta crystallogr ,sect b, 1983,
39,
480.
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