4lby
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Identifying ligand binding hot spots in proteins using brominated fragments== | |
| + | <StructureSection load='4lby' size='340' side='right'caption='[[4lby]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4lby]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LBY 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]] 2.692Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4lby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lby OCA], [https://pdbe.org/4lby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lby RCSB], [https://www.ebi.ac.uk/pdbsum/4lby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lby ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/EFTU1_THETH EFTU1_THETH] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | High-quality crystals of Thermus thermophilus EF-Tu in the GTP-bound conformation at 1.7-2.7 A resolution were used to test 18 small organic molecules, all brominated for confident identification in the anomalous difference maps. From this relatively small collection, it was possible to identify a small molecule bound in the functionally important tRNA CCA-end binding pocket. The antibiotic GE2270 A is known to interact with the same pocket in EF-Tu and to disrupt the association with tRNA. Bromide could be located from peaks in the anomalous map in data truncated to very low resolution without refining the structure. Considering the speed with which diffraction data can be collected today, it is proposed that it is worthwhile to collect the extra data from fragment screens while crystals are at hand to increase the knowledge of biological function and drug binding in an experimental structural context. | ||
| - | + | Identifying ligand-binding hot spots in proteins using brominated fragments.,Groftehauge MK, Therkelsen MO, Taaning R, Skrydstrup T, Morth JP, Nissen P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):1060-5. doi: , 10.1107/S1744309113018551. Epub 2013 Aug 19. PMID:23989163<ref>PMID:23989163</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4lby" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus]] | ||
| + | [[Category: Groftehauge MK]] | ||
| + | [[Category: Morth JP]] | ||
| + | [[Category: Nissen P]] | ||
| + | [[Category: Skrydstrup T]] | ||
| + | [[Category: Taaning R]] | ||
| + | [[Category: Therkelsen M]] | ||
Current revision
Identifying ligand binding hot spots in proteins using brominated fragments
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