2tbs | pdb_00002tbs

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

spinqualitylabelsall models 2tbs, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2tbs is a 1 chain structure with sequence from Salmo salar. This structure supersedes the now removed PDB entry 1tbs. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: BEN, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRY1_SALSA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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