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| | <StructureSection load='3moc' size='340' side='right'caption='[[3moc]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='3moc' size='340' side='right'caption='[[3moc]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3moc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MOC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3MOC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3moc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MOC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.82Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mnb|3mnb]], [[3mnc|3mnc]], [[3mns|3mns]], [[3mnx|3mnx]], [[3mo3|3mo3]], [[3mo6|3mo6]], [[3mo9|3mo9]], [[1gvk|1gvk]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </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=3moc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3moc OCA], [https://pdbe.org/3moc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3moc RCSB], [https://www.ebi.ac.uk/pdbsum/3moc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3moc 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=3moc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3moc OCA], [http://pdbe.org/3moc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3moc RCSB], [http://www.ebi.ac.uk/pdbsum/3moc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3moc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG]] Acts upon elastin. | + | [https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pancreatic elastase]] | |
| | [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| - | [[Category: Ginell, S]] | + | [[Category: Ginell S]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Joachimiak, G]] | + | [[Category: Joachimiak G]] |
| - | [[Category: Kim, Y]] | + | [[Category: Kim Y]] |
| - | [[Category: Petrova, T]] | + | [[Category: Petrova T]] |
| - | [[Category: Atomic resolution]]
| + | |
| - | [[Category: Disulfide bridge]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Radiation damage]]
| + | |
| Structural highlights
Function
CELA1_PIG Acts upon elastin.
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
Overall and site-specific X-ray-induced damage to porcine pancreatic elastase was studied at atomic resolution at temperatures of 100 and 15 K. The experiments confirmed that irradiation causes small movements of protein domains and bound water molecules in protein crystals. These structural changes occur not only at 100 K but also at temperatures as low as 15 K. An investigation of the deterioration of disulfide bridges demonstrated the following. (i) A decrease in the occupancy of S(gamma) atoms and the appearance of new cysteine rotamers occur simultaneously. (ii) The occupancy decrease is observed for all S(gamma) atoms, while new rotamers arise for some of the cysteine residues; the appearance of new conformations correlates with the accessibility to solvent. (iii) The sum of the occupancies of the initial and new conformations of a cysteine residue is approximately equal to the occupancy of the second cysteine residue in the bridge. (iv) The most pronounced changes occur at doses below 1.4 x 10(7) Gy, with only small changes occurring at higher doses. Comparison of the radiation-induced changes in an elastase crystal at 100 and 15 K suggested that the dose needed to induce a similar level of deterioration of the disulfide bonds and atomic displacements at 15 K to those seen at 100 K is more than two times higher.
X-ray-induced deterioration of disulfide bridges at atomic resolution.,Petrova T, Ginell S, Mitschler A, Kim Y, Lunin VY, Joachimiak G, Cousido-Siah A, Hazemann I, Podjarny A, Lazarski K, Joachimiak A Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1075-91. Epub 2010, Sep 18. PMID:20944241[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Petrova T, Ginell S, Mitschler A, Kim Y, Lunin VY, Joachimiak G, Cousido-Siah A, Hazemann I, Podjarny A, Lazarski K, Joachimiak A. X-ray-induced deterioration of disulfide bridges at atomic resolution. Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1075-91. Epub 2010, Sep 18. PMID:20944241 doi:10.1107/S0907444910033986
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