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3mty

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Comparison of the character and the speed of X-ray-induced structural changes of porcine pancreatic elastase at two temperatures, 100 and 15K. The data set was collected from region A of the crystal. First step of radiation damage

Structural highlights

3mty is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.101Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mty"

@@ Line 3: / Line 3: @@
 <StructureSection load='3mty' size='340' side='right'caption='[[3mty]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mty]] 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=3MTY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3MTY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mty]] 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=3MTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MTY 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]] 1.101&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gvk|1gvk]], [[3mnb|3mnb]], [[3mu0|3mu0]], [[3mu1|3mu1]], [[3mu4|3mu4]], [[3mu5|3mu5]], [[3mu8|3mu8]]</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=3mty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mty OCA], [https://pdbe.org/3mty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mty RCSB], [https://www.ebi.ac.uk/pdbsum/3mty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mty 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=3mty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mty OCA], [http://pdbe.org/3mty PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mty RCSB], [http://www.ebi.ac.uk/pdbsum/3mty PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mty ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Pancreatic elastase]]
 [[Category: Sus scrofa]]
-[[Category: Cousido-Siah, A]]
+[[Category: Cousido-Siah A]]
-[[Category: Ginell, S]]
+[[Category: Ginell S]]
-[[Category: Hazemann, I]]
+[[Category: Hazemann I]]
-[[Category: Joachimiak, A]]
+[[Category: Joachimiak A]]
-[[Category: Mitschler, A]]
+[[Category: Mitschler A]]
-[[Category: Petrova, T]]
+[[Category: Petrova T]]
-[[Category: Podjarny, A]]
+[[Category: Podjarny A]]
-[[Category: Atomic resolution]]
-[[Category: Disulfide bridge]]
-[[Category: Hydrolase]]
-[[Category: Radiation damage]]

3mty

From Proteopedia

Current revision

Comparison of the character and the speed of X-ray-induced structural changes of porcine pancreatic elastase at two temperatures, 100 and 15K. The data set was collected from region A of the crystal. First step of radiation damage

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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