1efu
From Proteopedia
(Difference between revisions)
m (Protected "1efu" [edit=sysop:move=sysop]) |
|||
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1efu.png|left|200px]] | ||
| - | + | ==ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI== | |
| - | + | <StructureSection load='1efu' size='340' side='right'caption='[[1efu]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1efu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The September 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Elongation Factors'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_9 10.2210/rcsb_pdb/mom_2006_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFU 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]] 2.5Å</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=1efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efu OCA], [https://pdbe.org/1efu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efu RCSB], [https://www.ebi.ac.uk/pdbsum/1efu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efu ProSAT]</span></td></tr> | |
| - | == | + | </table> |
| - | [[1efu]] is a 4 chain structure with sequence from [ | + | == Function == |
| + | [https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118] | ||
| + | == 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/ef/1efu_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/main_output.php?pdb_ID=1efu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Elongation factor|Elongation factor]] | *[[Elongation factor|Elongation factor]] | ||
| - | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | |
| - | + | __TOC__ | |
| - | < | + | </StructureSection> |
[[Category: Elongation Factors]] | [[Category: Elongation Factors]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
| - | [[Category: Berthet-Colominas | + | [[Category: Berthet-Colominas C]] |
| - | [[Category: Cusack | + | [[Category: Cusack S]] |
| - | [[Category: Kawashima | + | [[Category: Kawashima T]] |
| - | [[Category: Leberman | + | [[Category: Leberman R]] |
| - | [[Category: Wulff | + | [[Category: Wulff M]] |
| - | + | ||
Current revision
ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI
| |||||||||||
