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2bv3

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Crystal structure of a mutant elongation factor G trapped with a GTP analogue

Structural highlights

2bv3 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.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome.

Crystal structure of a mutant elongation factor G trapped with a GTP analogue.,Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT FEBS Lett. 2005 Aug 15;579(20):4492-7. PMID:16083884^[1]

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

References

↑ Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. Crystal structure of a mutant elongation factor G trapped with a GTP analogue. FEBS Lett. 2005 Aug 15;579(20):4492-7. PMID:16083884 doi:10.1016/j.febslet.2005.07.016

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/2bv3"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bv3' size='340' side='right'caption='[[2bv3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bv3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BV3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bv3]] is a 1 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=2BV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BV3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dar|1dar]], [[1efg|1efg]], [[1elo|1elo]], [[1fnm|1fnm]], [[1ip8|1ip8]], [[1ipm|1ipm]], [[1ipo|1ipo]], [[1ipr|1ipr]], [[1jqm|1jqm]], [[1jqs|1jqs]], [[1ktv|1ktv]], [[1pn6|1pn6]], [[2efg|2efg]], [[2bm1|2bm1]], [[2bm0|2bm0]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2bv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bv3 OCA], [http://pdbe.org/2bv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bv3 RCSB], [http://www.ebi.ac.uk/pdbsum/2bv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bv3 ProSAT]</span></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=2bv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bv3 OCA], [https://pdbe.org/2bv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bv3 RCSB], [https://www.ebi.ac.uk/pdbsum/2bv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bv3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EFG_THETH 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.
+[https://www.uniprot.org/uniprot/EFG_THETH 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 [[Category: Large Structures]]
-[[Category: Gudkov, A T]]
+[[Category: Thermus thermophilus]]
-[[Category: Hansson, S]]
+[[Category: Gudkov AT]]
-[[Category: Liljas, A]]
+[[Category: Hansson S]]
-[[Category: Logan, D T]]
+[[Category: Liljas A]]
-[[Category: Singh, R]]
+[[Category: Logan DT]]
-[[Category: Elongation factor]]
+[[Category: Singh R]]
-[[Category: Gtp-binding]]
-[[Category: Protein biosynthesis]]
-[[Category: Switch ii]]
-[[Category: Translation mutation thr84ala]]

2bv3

From Proteopedia

Current revision

Crystal structure of a mutant elongation factor G trapped with a GTP analogue

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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