1hj9
From Proteopedia
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| - | [[ | + | ==ATOMIC RESOLUTION STRUCTURES OF TRYPSIN PROVIDE INSIGHT INTO STRUCTURAL RADIATION DAMAGE== |
| + | <StructureSection load='1hj9' size='340' side='right' caption='[[1hj9]], [[Resolution|resolution]] 0.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hj9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HJ9 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANL:ANILINE'>ANL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aq7|1aq7]], [[1auj|1auj]], [[1az8|1az8]], [[1bju|1bju]], [[1bjv|1bjv]], [[1btp|1btp]], [[1c1n|1c1n]], [[1c1o|1c1o]], [[1c1p|1c1p]], [[1c1q|1c1q]], [[1c1r|1c1r]], [[1c1s|1c1s]], [[1c1t|1c1t]], [[1c2d|1c2d]], [[1c2e|1c2e]], [[1c2f|1c2f]], [[1c2g|1c2g]], [[1c2h|1c2h]], [[1c2i|1c2i]], [[1c2j|1c2j]], [[1c2k|1c2k]], [[1c2l|1c2l]], [[1c2m|1c2m]], [[1c5p|1c5p]], [[1c5q|1c5q]], [[1c5r|1c5r]], [[1c5s|1c5s]], [[1c5t|1c5t]], [[1c5u|1c5u]], [[1c5v|1c5v]], [[1c9t|1c9t]], [[1ce5|1ce5]], [[1cu7|1cu7]], [[1cu8|1cu8]], [[1cu9|1cu9]], [[1d6r|1d6r]], [[1ezx|1ezx]], [[1f0t|1f0t]], [[1f0u|1f0u]], [[1f2s|1f2s]], [[1g9i|1g9i]], [[1jrs|1jrs]], [[1jrt|1jrt]], [[1max|1max]], [[1may|1may]], [[1mts|1mts]], [[1mtu|1mtu]], [[1mtv|1mtv]], [[1mtw|1mtw]], [[1qa0|1qa0]], [[1qb1|1qb1]], [[1qb6|1qb6]], [[1qb9|1qb9]], [[1qbn|1qbn]], [[1qbo|1qbo]], [[1qcp|1qcp]], [[1ql7|1ql7]], [[1ql8|1ql8]], [[1sbw|1sbw]], [[1sfi|1sfi]], [[1taw|1taw]], [[1tio|1tio]], [[1xuf|1xuf]], [[1xug|1xug]], [[1xuh|1xuh]], [[1xui|1xui]], [[1xuj|1xuj]], [[1xuk|1xuk]], [[1yyy|1yyy]], [[1zzz|1zzz]], [[2btc|2btc]], [[2bza|2bza]], [[2tio|2tio]], [[3btd|3btd]], [[3bte|3bte]], [[3btf|3btf]], [[3btg|3btg]], [[3bth|3bth]], [[3btk|3btk]], [[3btm|3btm]], [[3btq|3btq]], [[3btt|3btt]], [[3btw|3btw]], [[5ptp|5ptp]]</td></tr> | ||
| + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hj9 RCSB], [http://www.ebi.ac.uk/pdbsum/1hj9 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hj9_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Radiation 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<ref>PMID:11264577</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Trypsin|Trypsin]] | *[[Trypsin|Trypsin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
Revision as of 09:50, 28 September 2014
ATOMIC RESOLUTION STRUCTURES OF TRYPSIN PROVIDE INSIGHT INTO STRUCTURAL RADIATION DAMAGE
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