1zo1

From Proteopedia

(Difference between revisions)

Revision as of 16:45, 10 April 2020

IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex

1zo1, resolution 13.80Å

Structural highlights

1zo1 is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1z03
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] [IF2_ECOLI] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.[HAMAP-Rule:MF_00100_B]

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

The 70S ribosome and its complement of factors required for initiation of translation in E. coli were purified separately and reassembled in vitro with GDPNP, producing a stable initiation complex (IC) stalled after 70S assembly. We have obtained a cryo-EM reconstruction of the IC showing IF2*GDPNP at the intersubunit cleft of the 70S ribosome. IF2*GDPNP contacts the 30S and 50S subunits as well as fMet-tRNA(fMet). IF2 here adopts a conformation radically different from that seen in the recent crystal structure of IF2. The C-terminal domain of IF2 binds to the single-stranded portion of fMet-tRNA(fMet), thereby forcing the tRNA into a novel orientation at the P site. The GTP binding domain of IF2 binds to the GTPase-associated center of the 50S subunit in a manner similar to EF-G and EF-Tu. Additionally, we present evidence for the localization of IF1, IF3, one C-terminal domain of L7/L12, and the N-terminal domain of IF2 in the initiation complex.

The cryo-EM structure of a translation initiation complex from Escherichia coli.,Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J Cell. 2005 Jun 3;121(5):703-12. PMID:15935757^[2]

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

References

↑ Pon CL, Wittmann-Liebold B, Gualerzi C. Structure--function relationships in Escherichia coli initiation factors. II. Elucidation of the primary structure of initiation factor IF-1. FEBS Lett. 1979 May 1;101(1):157-60. PMID:376343
↑ Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J. The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell. 2005 Jun 3;121(5):703-12. PMID:15935757 doi:10.1016/j.cell.2005.03.023

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/1zo1"

@@ Line 3: / Line 3: @@
 <SX load='1zo1' size='340' side='right' viewer='molstar' caption='[[1zo1]], [[Resolution|resolution]] 13.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zo1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZO1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zo1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZO1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZO1 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z03|1z03]]</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=1zo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo1 OCA], [http://pdbe.org/1zo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1zo1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zo1 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=1zo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo1 OCA], [http://pdbe.org/1zo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1zo1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zo1 ProSAT]</span></td></tr>
 </table>
 == Function ==

1zo1

From Proteopedia

Revision as of 16:45, 10 April 2020

IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex

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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