1ueb: Difference between revisions
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<StructureSection load='1ueb' size='340' side='right'caption='[[1ueb]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='1ueb' size='340' side='right'caption='[[1ueb]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ueb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ueb]] is a 2 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=1UEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UEB FirstGlance]. <br> | ||
</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=1ueb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueb OCA], [https://pdbe.org/1ueb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ueb RCSB], [https://www.ebi.ac.uk/pdbsum/1ueb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ueb ProSAT], [https://www.topsan.org/Proteins/RSGI/1ueb TOPSAN]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</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=1ueb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueb OCA], [https://pdbe.org/1ueb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ueb RCSB], [https://www.ebi.ac.uk/pdbsum/1ueb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ueb ProSAT], [https://www.topsan.org/Proteins/RSGI/1ueb TOPSAN]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/EFP_THET8 EFP_THET8] Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hanawa-Suetsugu | [[Category: Thermus thermophilus]] | ||
[[Category: Hori-Takemoto | [[Category: Hanawa-Suetsugu K]] | ||
[[Category: Kuramitsu | [[Category: Hori-Takemoto C]] | ||
[[Category: Kuramitsu S]] | |||
[[Category: Sakai | [[Category: Sakai H]] | ||
[[Category: Sekine | [[Category: Sekine S]] | ||
[[Category: Shirouzu | [[Category: Shirouzu M]] | ||
[[Category: Terada | [[Category: Terada T]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 02:51, 28 December 2023
Crystal structure of translation elongation factor P from Thermus thermophilus HB8Crystal structure of translation elongation factor P from Thermus thermophilus HB8
Structural highlights
FunctionEFP_THET8 Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity). 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 PubMedTranslation elongation factor P (EF-P) stimulates ribosomal peptidyltransferase activity. EF-P is conserved in bacteria and is essential for cell viability. Eukarya and Archaea have an EF-P homologue, eukaryotic initiation factor 5A (eIF-5A). In the present study, we determined the crystal structure of EF-P from Thermus thermophilus HB8 at a 1.65-A resolution. EF-P consists of three beta-barrel domains (I, II, and III), whereas eIF-5A has only two domains (N and C domains). Domain I of EF-P is topologically the same as the N domain of eIF-5A. On the other hand, EF-P domains II and III share the same topology as that of the eIF-5A C domain, indicating that domains II and III arose by duplication. Intriguingly, the N-terminal half of domain II and the C-terminal half of domain III of EF-P have sequence homologies to the N- and C-terminal halves, respectively, of the eIF-5A C domain. The three domains of EF-P are arranged in an "L" shape, with 65- and 53-A-long arms at an angle of 95 degrees, which is reminiscent of tRNA. Furthermore, most of the EF-P protein surface is negatively charged. Therefore, EF-P mimics the tRNA shape but uses domain topologies different from those of the known tRNA-mimicry translation factors. Domain I of EF-P has a conserved positive charge at its tip, like the eIF-5A N domain. Crystal structure of elongation factor P from Thermus thermophilus HB8.,Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9595-600. Epub 2004 Jun 21. PMID:15210970[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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