1okj: Difference between revisions
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New page: left|200px<br /><applet load="1okj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1okj, resolution 2.28Å" /> '''CRYSTAL STRUCTURE OF... |
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== | ==crystal structure of the essential E. coli YeaZ protein by MAD method using the gadolinium complex "DOTMA"== | ||
<StructureSection load='1okj' size='340' side='right'caption='[[1okj]], [[Resolution|resolution]] 2.28Å' scene=''> | |||
[[ | == Structural highlights == | ||
[[ | <table><tr><td colspan='2'>[[1okj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKJ FirstGlance]. <br> | ||
[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</td></tr> | ||
[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD3:GADOLINIUM+ION'>GD3</scene></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=1okj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okj OCA], [https://pdbe.org/1okj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okj RCSB], [https://www.ebi.ac.uk/pdbsum/1okj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okj ProSAT], [https://www.topsan.org/Proteins/BIGS/1okj TOPSAN]</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/ok/1okj_consurf.spt"</scriptWhenChecked> | ||
[[ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1okj ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A set of seven caged gadolinium complexes were used as vectors for introducing the chelated Gd(3+) ion into protein crystals in order to provide strong anomalous scattering for de novo phasing. The complexes contained multidentate ligand molecules with different functional groups to provide a panel of possible interactions with the protein. An exhaustive crystallographic analysis showed them to be nondisruptive to the diffraction quality of the prepared derivative crystals, and as many as 50% of the derivatives allowed the determination of accurate phases, leading to high-quality experimental electron-density maps. At least two successful derivatives were identified for all tested proteins. Structure refinement showed that the complexes bind to the protein surface or solvent-accessible cavities, involving hydrogen bonds, electrostatic and CH-pi interactions, explaining their versatile binding modes. Their high phasing power, complementary binding modes and ease of use make them highly suitable as a heavy-atom screen for high-throughput de novo structure determination, in combination with the SAD method. They can also provide a reliable tool for the development of new methods such as serial femtosecond crystallography. | |||
' | A complement to the modern crystallographer's toolbox: caged gadolinium complexes with versatile binding modes.,Stelter M, Molina R, Jeudy S, Kahn R, Abergel C, Hermoso JA Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1506-16. doi:, 10.1107/S1399004714005483. Epub 2014 May 23. PMID:24914962<ref>PMID:24914962</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1okj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Abergel C]] | |||
[[Category: Claverie JM]] | |||
[[Category: Jeudy S]] | |||