1hj8: Difference between revisions
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==1.00 AA | |||
==1.00 AA Trypsin from Atlantic Salmon== | |||
<StructureSection load='1hj8' size='340' side='right' caption='[[1hj8]], [[Resolution|resolution]] 1.00Å' scene=''> | <StructureSection load='1hj8' size='340' side='right' caption='[[1hj8]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bit|1bit]], [[1bzx|1bzx]], [[2sta|2sta]], [[2stb|2stb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bit|1bit]], [[1bzx|1bzx]], [[2sta|2sta]], [[2stb|2stb]]</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='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='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=1hj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj8 OCA], [http://pdbe.org/1hj8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hj8 RCSB], [http://www.ebi.ac.uk/pdbsum/1hj8 PDBsum]</span></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=1hj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj8 OCA], [http://pdbe.org/1hj8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hj8 RCSB], [http://www.ebi.ac.uk/pdbsum/1hj8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hj8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hj8_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hj8_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1hj8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1hj8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:29, 10 January 2018
1.00 AA Trypsin from Atlantic Salmon1.00 AA Trypsin from Atlantic Salmon
Structural highlights
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 PubMedRadiation damage is an inherent problem in protein X-ray crystallography and the process has recently been shown to be highly specific, exhibiting features such as cleavage of disulfide bonds, decarboxylation of acidic residues, increase in atomic B factors and increase in unit-cell volume. Reported here are two trypsin structures at atomic resolution (1.00 and 0.95 A), the data for which were collected at a third-generation synchrotron (ESRF) at two different beamlines. Both trypsin structures exhibit broken disulfide bonds; in particular, the bond from Cys191 to Cys220 is very sensitive to synchrotron radiation. The data set collected at the most intense beamline (ID14-EH4) shows increased structural radiation damage in terms of lower occupancies for cysteine residues, more breakage in the six disulfide bonds and more alternate conformations. It appears that high intensity and not only the total X-ray dose is most harmful to protein crystals. Atomic resolution structures of trypsin provide insight into structural radiation damage.,Leiros HK, McSweeney SM, Smalas AO Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):488-97. PMID:11264577[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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