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| | ==The Crystal Structure of LepA== | | ==The Crystal Structure of LepA== |
| - | <StructureSection load='3cb4' size='340' side='right' caption='[[3cb4]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3cb4' size='340' side='right'caption='[[3cb4]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cb4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CB4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CB4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cb4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CB4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lepA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3cb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cb4 OCA], [http://pdbe.org/3cb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cb4 RCSB], [http://www.ebi.ac.uk/pdbsum/3cb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cb4 ProSAT]</span></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=3cb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cb4 OCA], [https://pdbe.org/3cb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cb4 RCSB], [https://www.ebi.ac.uk/pdbsum/3cb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cb4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LEPA_ECOLI LEPA_ECOLI]] Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.<ref>PMID:17110332</ref> <ref>PMID:20045415</ref> | + | [[https://www.uniprot.org/uniprot/LEPA_ECOLI LEPA_ECOLI]] Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.<ref>PMID:17110332</ref> <ref>PMID:20045415</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Elongation factor|Elongation factor]] | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | *[[Escherichia coli LepA%2C the ribosomal back translocase|Escherichia coli LepA%2C the ribosomal back translocase]] | | *[[Escherichia coli LepA%2C the ribosomal back translocase|Escherichia coli LepA%2C the ribosomal back translocase]] |
| - | *[[GTP-binding protein|GTP-binding protein]] | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Bailey, S]] | | [[Category: Bailey, S]] |
| | [[Category: Blaha, G]] | | [[Category: Blaha, G]] |
| Structural highlights
Function
[LEPA_ECOLI] Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.[1] [2]
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 PubMed
LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-A resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However, the orientation of domains III and V in LepA differs from their orientations in EF-G. LepA also contains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold. The high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA bound to the ribosome using a 7.3-A cryo-EM structure of a complex between EF-G and the 70S ribosome. In this model, the very electrostatically positive CTD of LepA is placed in the direct vicinity of the A site of the large ribosomal subunit, suggesting a possible interaction between the CTD and the back translocated tRNA or 23S rRNA.
The structure of LepA, the ribosomal back translocase.,Evans RN, Blaha G, Bailey S, Steitz TA Proc Natl Acad Sci U S A. 2008 Mar 25;105(12):4673-8. Epub 2008 Mar 24. PMID:18362332[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Qin Y, Polacek N, Vesper O, Staub E, Einfeldt E, Wilson DN, Nierhaus KH. The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell. 2006 Nov 17;127(4):721-33. PMID:17110332 doi:http://dx.doi.org/10.1016/j.cell.2006.09.037
- ↑ Liu H, Pan D, Pech M, Cooperman BS. Interrupted catalysis: the EF4 (LepA) effect on back-translocation. J Mol Biol. 2010 Mar 5;396(4):1043-52. doi: 10.1016/j.jmb.2009.12.043. Epub 2010 , Jan 4. PMID:20045415 doi:http://dx.doi.org/10.1016/j.jmb.2009.12.043
- ↑ Evans RN, Blaha G, Bailey S, Steitz TA. The structure of LepA, the ribosomal back translocase. Proc Natl Acad Sci U S A. 2008 Mar 25;105(12):4673-8. Epub 2008 Mar 24. PMID:18362332
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