1a0j

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(New page: 200px<br /><applet load="1a0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a0j, resolution 1.7&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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caption="1a0j, resolution 1.7&Aring;" />
'''CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED FISH SPECIES.'''<br />
'''CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED FISH SPECIES.'''<br />
==Overview==
==Overview==
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The crystal structure of cationic trypsin (CST) from the Atlantic salmon, (Salmo salar) has been refined at 1.70 A resolution. The crystals are, orthorhombic, belong to space group P212121, with lattice parameters a =, 65.91, b = 83.11 and c = 154.79 A, and comprise four molecules per, asymmetric unit. The structure was solved by molecular replacement with, AMoRe and refined with X-PLOR to an R value of 17.4% and Rfree of 21.5%, for reflections |F| &gt; 3sigmaF between 8.0 and 1.7 A resolution. The four, non-crystallographic symmetry (NCS) related molecules in the asymmetric, unit display r.m.s. deviations in the range 0.31-0.74 A for main-chain, atoms, with the largest differences confined to two loops. One of these is, the calcium-binding loop where the electron-density indicates a calcium, ion for only one of the four molecules. In order to find structural, rationalizations for the observed difference in thermostability and, catalytic efficiency of CST, anionic salmon trypsin (AST) and bovine, trypsin (BT), the three structures have been extensively compared. The, largest deviations for the superimposed structures occur in the surface, loops and particularly in the so-called 'autolysis loop'. Both the salmon, enzymes possess a high methionine content, lower overall hydrophobicity, and enhanced surface hydrophilicity, compared with BT. These properties, have so far been correlated to cold-adaptation features, while in this, work it is shown that the non-psychrophilic cationic salmon trypsin shares, these features with the psychrophilic anionic salmon trypsin.
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The crystal structure of cationic trypsin (CST) from the Atlantic salmon (Salmo salar) has been refined at 1.70 A resolution. The crystals are orthorhombic, belong to space group P212121, with lattice parameters a = 65.91, b = 83.11 and c = 154.79 A, and comprise four molecules per asymmetric unit. The structure was solved by molecular replacement with AMoRe and refined with X-PLOR to an R value of 17.4% and Rfree of 21.5% for reflections |F| &gt; 3sigmaF between 8.0 and 1.7 A resolution. The four non-crystallographic symmetry (NCS) related molecules in the asymmetric unit display r.m.s. deviations in the range 0.31-0.74 A for main-chain atoms, with the largest differences confined to two loops. One of these is the calcium-binding loop where the electron-density indicates a calcium ion for only one of the four molecules. In order to find structural rationalizations for the observed difference in thermostability and catalytic efficiency of CST, anionic salmon trypsin (AST) and bovine trypsin (BT), the three structures have been extensively compared. The largest deviations for the superimposed structures occur in the surface loops and particularly in the so-called 'autolysis loop'. Both the salmon enzymes possess a high methionine content, lower overall hydrophobicity and enhanced surface hydrophilicity, compared with BT. These properties have so far been correlated to cold-adaptation features, while in this work it is shown that the non-psychrophilic cationic salmon trypsin shares these features with the psychrophilic anionic salmon trypsin.
==About this Structure==
==About this Structure==
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1A0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmo_salar Salmo salar] with CA, SO4 and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A0J OCA].
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1A0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmo_salar Salmo salar] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BEN:'>BEN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trypsin]]
[[Category: Trypsin]]
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[[Category: Schroeder, H.K.]]
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[[Category: Schroeder, H K.]]
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[[Category: Smalaas, A.O.]]
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[[Category: Smalaas, A O.]]
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[[Category: Willassen, N.P.]]
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[[Category: Willassen, N P.]]
[[Category: BEN]]
[[Category: BEN]]
[[Category: CA]]
[[Category: CA]]
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[[Category: trypsin]]
[[Category: trypsin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:31:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:36 2008''

Revision as of 09:39, 21 February 2008


1a0j, resolution 1.7Å

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CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED FISH SPECIES.

Overview

The crystal structure of cationic trypsin (CST) from the Atlantic salmon (Salmo salar) has been refined at 1.70 A resolution. The crystals are orthorhombic, belong to space group P212121, with lattice parameters a = 65.91, b = 83.11 and c = 154.79 A, and comprise four molecules per asymmetric unit. The structure was solved by molecular replacement with AMoRe and refined with X-PLOR to an R value of 17.4% and Rfree of 21.5% for reflections |F| > 3sigmaF between 8.0 and 1.7 A resolution. The four non-crystallographic symmetry (NCS) related molecules in the asymmetric unit display r.m.s. deviations in the range 0.31-0.74 A for main-chain atoms, with the largest differences confined to two loops. One of these is the calcium-binding loop where the electron-density indicates a calcium ion for only one of the four molecules. In order to find structural rationalizations for the observed difference in thermostability and catalytic efficiency of CST, anionic salmon trypsin (AST) and bovine trypsin (BT), the three structures have been extensively compared. The largest deviations for the superimposed structures occur in the surface loops and particularly in the so-called 'autolysis loop'. Both the salmon enzymes possess a high methionine content, lower overall hydrophobicity and enhanced surface hydrophilicity, compared with BT. These properties have so far been correlated to cold-adaptation features, while in this work it is shown that the non-psychrophilic cationic salmon trypsin shares these features with the psychrophilic anionic salmon trypsin.

About this Structure

1A0J is a Single protein structure of sequence from Salmo salar with , and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

Structure of a non-psychrophilic trypsin from a cold-adapted fish species., Schroder HK, Willassen NP, Smalas AO, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):780-98. PMID:9757092

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