1pn6

From Proteopedia

(Difference between revisions)

Revision as of 16:36, 10 April 2020

Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.

1pn6, resolution 10.80Å

Structural highlights

1pn6 is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1fnm, 1pn7, 1pn8
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EFG_THETH] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

During the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratchet-like rotation of the 30S subunit relative to the 50S subunit in the direction of the mRNA movement. By means of cryo-electron microscopy we observe that this rotation is accompanied by a 20 A movement of the L1 stalk of the 50S subunit, implying that this region is involved in the translocation of deacylated tRNAs from the P to the E site. These ribosomal motions can occur only when the P-site tRNA is deacylated. Prior to peptidyl-transfer to the A-site tRNA or peptide removal, the presence of the charged P-site tRNA locks the ribosome and prohibits both of these motions.

Locking and unlocking of ribosomal motions.,Valle M, Zavialov A, Sengupta J, Rawat U, Ehrenberg M, Frank J Cell. 2003 Jul 11;114(1):123-34. PMID:12859903^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Valle M, Zavialov A, Sengupta J, Rawat U, Ehrenberg M, Frank J. Locking and unlocking of ribosomal motions. Cell. 2003 Jul 11;114(1):123-34. PMID:12859903

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pn6"

@@ Line 3: / Line 3: @@
 <SX load='1pn6' size='340' side='right' viewer='molstar' caption='[[1pn6]], [[Resolution|resolution]] 10.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PN6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PN6 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fnm|1fnm]], [[1pn7|1pn7]], [[1pn8|1pn8]]</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=1pn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn6 OCA], [http://pdbe.org/1pn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pn6 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn6 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn6 OCA], [http://pdbe.org/1pn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pn6 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn6 ProSAT]</span></td></tr>
 </table>
 == Function ==

1pn6

From Proteopedia

Revision as of 16:36, 10 April 2020

Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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