2bm0: Difference between revisions

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~~{{Seed}}~~

~~[[Image:2bm0.png|left|200px]]~~

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==Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant T84A==

~~The line below this paragraph~~, ~~containing~~ "~~STRUCTURE_2bm0~~"~~, creates the~~ "~~Structure Box~~" ~~on the page~~.

~~You may change~~ the ~~PDB parameter (which sets~~ the ~~PDB file loaded into~~ the ~~applet~~)

== Structural highlights ==

or the ~~SCENE parameter~~ (~~which sets~~ the ~~initial scene displayed when~~ the ~~page is loaded)~~,

<table><tr><td colspan='2'>[[2bm0]] 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=2BM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BM0 FirstGlance]. <br>

~~or leave~~ the ~~SCENE parameter empty for~~ the ~~default display~~.

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr>

-->

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

~~{{STRUCTURE_2bm0| PDB~~=~~2bm0 | SCENE~~= }}

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm0 OCA], [https://pdbe.org/2bm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bm0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bm0 ProSAT]</span></td></tr>

</table>

== Function ==

[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]]

Check<jmol>

<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/2bm0_consurf.spt"</scriptWhenChecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>

<text>to colour the structure by Evolutionary Conservation</text>

</jmolCheckbox>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bm0 ConSurf].

== Publication Abstract from PubMed ==

Fusidic acid (FA) is a steroid antibiotic commonly used against Gram positive bacterial infections. It inhibits protein synthesis by stalling elongation factor G (EF-G) on the ribosome after translocation. A significant number of the mutations conferring strong FA resistance have been mapped at the interfaces between domains G, III and V of EF-G. However, direct information on how such mutations affect the structure has hitherto not been available. Here we present the crystal structures of two mutants of Thermus thermophilus EF-G, G16V and T84A, which exhibit FA hypersensitivity and resistance in vitro, respectively. These mutants also have higher and lower affinity for GTP respectively than wild-type EF-G. The mutations cause significant conformational changes in the switch II loop that have opposite effects on the position of a key residue, Phe90, which undergoes large conformational changes. This correlates with the importance of Phe90 in FA sensitivity reported in previous studies. These structures substantiate the importance of the domain G/domain III/domain V interfaces as a key component of the FA binding site. The mutations also cause subtle changes in the environment of the "P-loop lysine", Lys25. This led us to examine the conformation of the equivalent residue in all structures of translational GTPases, which revealed that EF-G and eEF2 form a group separate from the others and suggested that the role of Lys25 may be different in the two groups.

~~===RIBOSOMAL ELONGATION FACTOR G (~~EF-G) ~~FUSIDIC ACID RESISTANT MUTANT T84A===~~

Structural insights into fusidic acid resistance and sensitivity in EF-G.,Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT J Mol Biol. 2005 May 13;348(4):939-49. PMID:15843024<ref>PMID:15843024</ref>

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

</div>

~~<!--~~

==See Also==

~~The line below this paragraph, {{ABSTRACT_PUBMED_15843024}}, adds the Publication Abstract to the page~~

*[[Elongation factor 3D structures|Elongation factor 3D structures]]

~~(as it appears on PubMed at http://www.pubmed.gov), where 15843024 is the PubMed ID number.~~

== References ==

~~-->~~

~~{{ABSTRACT_PUBMED_15843024}}~~

__TOC__

</StructureSection>

==~~About this Structure~~==

[[Category: Large Structures]]

~~2BM0 is a~~ [[~~Single protein]] structure of 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=2BM0 OCA~~].

==~~Reference~~==

~~Structural insights into fusidic acid resistance and sensitivity in EF-G., Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT, J Mol Biol. 2005 May 13;348(4):939-49. PMID:[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15843024 15843024]~~

[[Category: ~~Single protein~~]]

[[Category: Thermus thermophilus]]

[[Category: Gudkov~~, A T.~~]]

[[Category: Gudkov AT]]

[[Category: Hansson, S.]]

[[Category: Hansson S]]

[[Category: Liljas, A.]]

[[Category: Liljas A]]

[[Category: Logan~~, D T.~~]]

[[Category: Logan DT]]

[[Category: Singh, R~~.]]~~

[[Category: Singh R]]

~~[[Category: Elongation factor]]~~

~~[[Category: Gtp-binding~~]]

~~[[Category: Protein biosynthesis]]~~

~~[[Category: Switch ii]]~~

~~[[Category: Translation mutation thr84ala]]~~

~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:04:14 2008''~~

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@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2bm0.png|left|200px]]
-<!--
+==Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant T84A==
-The line below this paragraph, containing "STRUCTURE_2bm0", creates the "Structure Box" on the page.
+<StructureSection load='2bm0' size='340' side='right'caption='[[2bm0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2bm0]] 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=2BM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BM0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_2bm0|  PDB=2bm0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm0 OCA], [https://pdbe.org/2bm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bm0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bm0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/2bm0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bm0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fusidic acid (FA) is a steroid antibiotic commonly used against Gram positive bacterial infections. It inhibits protein synthesis by stalling elongation factor G (EF-G) on the ribosome after translocation. A significant number of the mutations conferring strong FA resistance have been mapped at the interfaces between domains G, III and V of EF-G. However, direct information on how such mutations affect the structure has hitherto not been available. Here we present the crystal structures of two mutants of Thermus thermophilus EF-G, G16V and T84A, which exhibit FA hypersensitivity and resistance in vitro, respectively. These mutants also have higher and lower affinity for GTP respectively than wild-type EF-G. The mutations cause significant conformational changes in the switch II loop that have opposite effects on the position of a key residue, Phe90, which undergoes large conformational changes. This correlates with the importance of Phe90 in FA sensitivity reported in previous studies. These structures substantiate the importance of the domain G/domain III/domain V interfaces as a key component of the FA binding site. The mutations also cause subtle changes in the environment of the "P-loop lysine", Lys25. This led us to examine the conformation of the equivalent residue in all structures of translational GTPases, which revealed that EF-G and eEF2 form a group separate from the others and suggested that the role of Lys25 may be different in the two groups.
-===RIBOSOMAL ELONGATION FACTOR G (EF-G) FUSIDIC ACID RESISTANT MUTANT T84A===
+Structural insights into fusidic acid resistance and sensitivity in EF-G.,Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT J Mol Biol. 2005 May 13;348(4):939-49. PMID:15843024<ref>PMID:15843024</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bm0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15843024}}, adds the Publication Abstract to the page
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15843024 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15843024}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-BM0 is a [[Single protein]] structure of 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=2BM0 OCA].
-==Reference==
-Structural insights into fusidic acid resistance and sensitivity in EF-G., Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT, J Mol Biol. 2005 May 13;348(4):939-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15843024 15843024]
-[[Category: Single protein]]
 [[Category: Thermus thermophilus]]
-[[Category: Gudkov, A T.]]
+[[Category: Gudkov AT]]
-[[Category: Hansson, S.]]
+[[Category: Hansson S]]
-[[Category: Liljas, A.]]
+[[Category: Liljas A]]
-[[Category: Logan, D T.]]
+[[Category: Logan DT]]
-[[Category: Singh, R.]]
+[[Category: Singh R]]
-[[Category: Elongation factor]]
-[[Category: Gtp-binding]]
-[[Category: Protein biosynthesis]]
-[[Category: Switch ii]]
-[[Category: Translation mutation thr84ala]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:04:14 2008''