2tbs

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|PDB= 2tbs |SIZE=350|CAPTION= <scene name='initialview01'>2tbs</scene>, resolution 1.8&Aring;
|PDB= 2tbs |SIZE=350|CAPTION= <scene name='initialview01'>2tbs</scene>, resolution 1.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>
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|LIGAND= <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2tbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tbs OCA], [http://www.ebi.ac.uk/pdbsum/2tbs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2tbs RCSB]</span>
}}
}}
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[[Category: Trypsin]]
[[Category: Trypsin]]
[[Category: Smalas, A O.]]
[[Category: Smalas, A O.]]
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[[Category: BEN]]
 
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[[Category: CA]]
 
[[Category: hydrolase(serine proteinase)]]
[[Category: hydrolase(serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:03:31 2008''

Revision as of 02:03, 31 March 2008


PDB ID 2tbs

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: ,
Activity: Trypsin, with EC number 3.4.21.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



COLD-ADAPTION OF ENZYMES: STRUCTURAL COMPARISON BETWEEN SALMON AND BOVINE TRYPSINS


Overview

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.

About this Structure

2TBS is a Single protein structure of sequence from Salmo salar. This structure supersedes the now removed PDB entry 1TBS. Full crystallographic information is available from OCA.

Reference

Cold adaption of enzymes: structural comparison between salmon and bovine trypsins., Smalas AO, Heimstad ES, Hordvik A, Willassen NP, Male R, Proteins. 1994 Oct;20(2):149-66. PMID:7846025

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