2iu1

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of eIF5 C-terminal domain

Structural highlights

2iu1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IF5_HUMAN Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).

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 carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively.

The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5.,Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736^[1]

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

References

↑ Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U. The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736 doi:http://dx.doi.org/10.1016/j.jmb.2006.05.021

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/2iu1"

Categories: Homo sapiens | Large Structures | Baumann U | Bieniossek C | Schuetz P

@@ Line 3: / Line 3: @@
 <StructureSection load='2iu1' size='340' side='right'caption='[[2iu1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iu1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IU1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iu1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IU1 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=2iu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu1 OCA], [https://pdbe.org/2iu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iu1 RCSB], [https://www.ebi.ac.uk/pdbsum/2iu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iu1 ProSAT]</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]] 1.8&#8491;</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=2iu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu1 OCA], [https://pdbe.org/2iu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iu1 RCSB], [https://www.ebi.ac.uk/pdbsum/2iu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iu1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/IF5_HUMAN IF5_HUMAN]] Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
+[https://www.uniprot.org/uniprot/IF5_HUMAN IF5_HUMAN] Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Baumann, U]]
+[[Category: Baumann U]]
-[[Category: Bieniossek, C]]
+[[Category: Bieniossek C]]
-[[Category: Schuetz, P]]
+[[Category: Schuetz P]]
-[[Category: Eif5]]
-[[Category: Gtp-binding]]
-[[Category: Initiation factor]]
-[[Category: Mfc]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphorylation]]
-[[Category: Protein biosynthesis]]
-[[Category: Transcription]]
-[[Category: Translation inititation]]

2iu1

From Proteopedia

Current revision

Crystal structure of eIF5 C-terminal domain

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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