1d1n

From Proteopedia

(Difference between revisions)

Revision as of 10:42, 14 July 2021

SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2

Structural highlights

1d1n is a 1 chain structure with sequence from Atcc 12980. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IF2_GEOSE] 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.

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

The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel beta-strands, connected via loops, and forms a closed beta-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu small middle dotaminoacyl-tRNA small middle dot GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.

Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2.,Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R EMBO J. 2000 Apr 17;19(8):1918-26. PMID:10775275^[1]

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

References

↑ Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R. Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2. EMBO J. 2000 Apr 17;19(8):1918-26. PMID:10775275 doi:10.1093/emboj/19.8.1918

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d1n"

@@ Line 3: / Line 3: @@
 <StructureSection load='1d1n' size='340' side='right'caption='[[1d1n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1d1n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D1N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1d1n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D1N FirstGlance]. <br>
-</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=1d1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1n OCA], [http://pdbe.org/1d1n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d1n RCSB], [http://www.ebi.ac.uk/pdbsum/1d1n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1n ProSAT]</span></td></tr>
+</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=1d1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1n OCA], [https://pdbe.org/1d1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d1n RCSB], [https://www.ebi.ac.uk/pdbsum/1d1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IF2_GEOSE IF2_GEOSE]] 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.
+[[https://www.uniprot.org/uniprot/IF2_GEOSE IF2_GEOSE]] 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1d1n

From Proteopedia

Revision as of 10:42, 14 July 2021

SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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