|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==COLD-ADAPTION OF ENZYMES: STRUCTURAL COMPARISON BETWEEN SALMON AND BOVINE TRYPSINS== | | ==COLD-ADAPTION OF ENZYMES: STRUCTURAL COMPARISON BETWEEN SALMON AND BOVINE TRYPSINS== |
| - | <StructureSection load='2tbs' size='340' side='right' caption='[[2tbs]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='2tbs' size='340' side='right'caption='[[2tbs]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2tbs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atlantic_salmon Atlantic salmon]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tbs 1tbs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TBS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TBS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2tbs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmo_salar Salmo salar]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tbs 1tbs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TBS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2tbs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2tbs RCSB], [http://www.ebi.ac.uk/pdbsum/2tbs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2tbs ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2tbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tbs OCA], [https://pdbe.org/2tbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tbs RCSB], [https://www.ebi.ac.uk/pdbsum/2tbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tbs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TRY1_SALSA TRY1_SALSA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Trypsin|Trypsin]] | + | *[[Trypsin 3D structures|Trypsin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atlantic salmon]] | + | [[Category: Large Structures]] |
| - | [[Category: Trypsin]] | + | [[Category: Salmo salar]] |
| - | [[Category: Smalas, A O]] | + | [[Category: Smalas AO]] |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Smalas AO, Heimstad ES, Hordvik A, Willassen NP, Male R. Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Proteins. 1994 Oct;20(2):149-66. PMID:7846025 doi:http://dx.doi.org/10.1002/prot.340200205
|
