1ah9: Difference between revisions
m Protected "1ah9" [edit=sysop:move=sysop] |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES== | |||
<StructureSection load='1ah9' size='340' side='right'caption='[[1ah9]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ah9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AH9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ah9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ah9 OCA], [https://pdbe.org/1ah9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ah9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ah9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ah9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IF1_ECOLI IF1_ECOLI] No specific function has so far been attributed to this initiation factor; however, it seems to stimulate more or less all the activities of the other two initiation factors, IF-2 and IF-3.<ref>PMID:376343</ref> | |||
== 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/ah/1ah9_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=1ah9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of the translational initiation factor IF1 from Escherichia coli has been determined with multidimensional NMR spectroscopy. Using 1041 distance and 78 dihedral constraints, 40 distance geometry structures were calculated, which were refined by restrained molecular dynamics. From this set, 19 structures were selected, having low constraint energy and few constraint violations. The ensemble of 19 structures displays a root-mean-square deviation versus the average of 0.49 A for the backbone atoms and 1.12 A for all atoms for residues 6-36 and 46-67. The structure of IF1 is characterized by a five-stranded beta-barrel. The loop connecting strands three and four contains a short 3(10) helix but this region shows considerably higher flexibility than the beta-barrel. The fold of IF1 is very similar to that found in the bacterial cold shock proteins CspA and CspB, the N-terminal domain of aspartyl-tRNA synthetase and the staphylococcal nuclease, and can be identified as the oligomer-binding motif. Several proteins of this family are nucleic acid-binding proteins. This suggests that IF1 plays its role in the initiation of protein synthesis by nucleic acid interactions. Specific changes of NMR signals of IF1 upon titration with 30S ribosomal subunit identifies several residues that are involved in the interaction with ribosomes. | |||
The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif.,Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R EMBO J. 1997 Mar 17;16(6):1436-43. PMID:9135158<ref>PMID:9135158</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ah9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Boelens | [[Category: Large Structures]] | ||
[[Category: Gualerzi | [[Category: Boelens R]] | ||
[[Category: Kaptein | [[Category: Gualerzi CO]] | ||
[[Category: Paci | [[Category: Kaptein R]] | ||
[[Category: Sette | [[Category: Paci M]] | ||
[[Category: Spurio | [[Category: Sette M]] | ||
[[Category: Tilborg | [[Category: Spurio R]] | ||
[[Category: Van Tilborg P]] | |||
Latest revision as of 11:13, 22 May 2024
THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURESTHE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES
Structural highlights
FunctionIF1_ECOLI No specific function has so far been attributed to this initiation factor; however, it seems to stimulate more or less all the activities of the other two initiation factors, IF-2 and IF-3.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the translational initiation factor IF1 from Escherichia coli has been determined with multidimensional NMR spectroscopy. Using 1041 distance and 78 dihedral constraints, 40 distance geometry structures were calculated, which were refined by restrained molecular dynamics. From this set, 19 structures were selected, having low constraint energy and few constraint violations. The ensemble of 19 structures displays a root-mean-square deviation versus the average of 0.49 A for the backbone atoms and 1.12 A for all atoms for residues 6-36 and 46-67. The structure of IF1 is characterized by a five-stranded beta-barrel. The loop connecting strands three and four contains a short 3(10) helix but this region shows considerably higher flexibility than the beta-barrel. The fold of IF1 is very similar to that found in the bacterial cold shock proteins CspA and CspB, the N-terminal domain of aspartyl-tRNA synthetase and the staphylococcal nuclease, and can be identified as the oligomer-binding motif. Several proteins of this family are nucleic acid-binding proteins. This suggests that IF1 plays its role in the initiation of protein synthesis by nucleic acid interactions. Specific changes of NMR signals of IF1 upon titration with 30S ribosomal subunit identifies several residues that are involved in the interaction with ribosomes. The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif.,Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R EMBO J. 1997 Mar 17;16(6):1436-43. PMID:9135158[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||