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| | <StructureSection load='2pu3' size='340' side='right'caption='[[2pu3]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='2pu3' size='340' side='right'caption='[[2pu3]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alisl Alisl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PU3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2PU3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_salmonicida_LFI1238 Aliivibrio salmonicida LFI1238]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PU3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g7e|2g7e]], [[2g7f|2g7f]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </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=2pu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pu3 OCA], [https://pdbe.org/2pu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pu3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pu3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2pu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pu3 OCA], [http://pdbe.org/2pu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pu3 RCSB], [http://www.ebi.ac.uk/pdbsum/2pu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pu3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2XSL7_ALISL Q2XSL7_ALISL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pu/2pu3_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pu/2pu3_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alisl]] | + | [[Category: Aliivibrio salmonicida LFI1238]] |
| - | [[Category: Deoxyribonuclease I]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altermark, B]] | + | [[Category: Altermark B]] |
| - | [[Category: Helland, R]] | + | [[Category: Helland R]] |
| - | [[Category: Moe, E]] | + | [[Category: Moe E]] |
| - | [[Category: Smalas, A O]] | + | [[Category: Smalas AO]] |
| - | [[Category: Willassen, N P]] | + | [[Category: Willassen NP]] |
| - | [[Category: Cold adaptation]]
| + | |
| - | [[Category: Endonuclease i]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Psychrophilic enzyme]]
| + | |
| - | [[Category: Salt adaptation]]
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| Structural highlights
Function
Q2XSL7_ALISL
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 the periplasmic/extracellular endonuclease I from Vibrio salmonicida has been solved to 1.5 A resolution and, in comparison to the corresponding endonucleases from V. cholerae and V. vulnificus, serves as a model system for the investigation of the structural determinants involved in the temperature and NaCl adaptation of this enzyme class. The overall fold of the three enzymes is essentially similar, but the V. salmonicida endonuclease displays a significantly more positive surface potential than the other two enzymes owing to the presence of ten more Lys residues. However, if the optimum salt concentrations for the V. salmonicida and V. cholerae enzymes are taken into consideration in the electrostatic surface-potential calculation, the potentials of the two enzymes become surprisingly similar. The higher number of basic residues in the V. salmonicida protein is therefore likely to be a result, at least in part, of adaptation to the more saline habitat of V. salmonicida (seawater) than V. cholerae (brackish water). The hydrophobic core of all three enzymes is almost identical, but the V. salmonicida endonuclease has a slightly lower number of internal hydrogen bonds. This, together with repulsive forces between the basic residues on the protein surface of V. salmonicida endonuclease I and differences in the distribution of salt bridges, probably results in higher flexibility of regions of the V. salmonicida protein. This is likely to influence both the catalytic activity and the stability of the protein.
Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida.,Altermark B, Helland R, Moe E, Willassen NP, Smalas AO Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):368-76. Epub 2008, Mar 19. PMID:18391403[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Altermark B, Helland R, Moe E, Willassen NP, Smalas AO. Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida. Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):368-76. Epub 2008, Mar 19. PMID:18391403 doi:10.1107/S0907444908000097
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