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2xre
From Proteopedia
(Difference between revisions)
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| - | + | ==Detection of cobalt in previously unassigned human SENP1 structure== | |
| - | + | <StructureSection load='2xre' size='340' side='right' caption='[[2xre]], [[Resolution|resolution]] 2.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2xre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iyd|2iyd]], [[2iyc|2iyc]], [[2iy1|2iy1]], [[2iy0|2iy0]], [[2ckg|2ckg]], [[2xph|2xph]], [[2g4d|2g4d]], [[2ckh|2ckh]]</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=2xre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xre RCSB], [http://www.ebi.ac.uk/pdbsum/2xre 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/xr/2xre_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 == | ||
| + | Metal ions often stabilize intermolecular contacts between macromolecules, thereby promoting crystallization. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation was noted. This was assigned as Co(2+), an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggested that Co(2+) had been overlooked and re-refinement supported this conclusion. High-throughput automated re-refinement protocols also failed to mark the Co(2+) position, supporting the requirement for the incorporation of as much information as possible to enhance the value of such protocols. | ||
| - | + | The role of Co(2)+ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols.,Rimsa V, Eadsforth T, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):442-5. Epub, 2011 Mar 24. PMID:21505236<ref>PMID:21505236</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Sentrin-specific protease|Sentrin-specific protease]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Eadsforth, T | + | [[Category: Eadsforth, T]] |
| - | [[Category: Hay, R T | + | [[Category: Hay, R T]] |
| - | [[Category: Hunter, W N | + | [[Category: Hunter, W N]] |
| - | [[Category: Rimsa, V | + | [[Category: Rimsa, V]] |
[[Category: Cysteine protease]] | [[Category: Cysteine protease]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 06:30, 21 December 2014
Detection of cobalt in previously unassigned human SENP1 structure
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Categories: Human | Eadsforth, T | Hay, R T | Hunter, W N | Rimsa, V | Cysteine protease | Hydrolase

