1fnm

<StructureSection load='1fnm' size='340' side='right' caption='[[1fnm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fnm]] 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=1FNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FNM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=1fnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fnm OCA], [http://pdbe.org/1fnm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fnm RCSB], [http://www.ebi.ac.uk/pdbsum/1fnm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fnm ProSAT]</span></td></tr>

[[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.

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== Publication Abstract from PubMed ==

The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EF-G domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.,Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A J Mol Biol. 2000 Nov 3;303(4):593-603. PMID:11054294<ref>PMID:11054294</ref>

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

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<div class="pdbe-citations 1fnm" style="background-color:#fffaf0;"></div>

*[[Elongation factor|Elongation factor]]

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Gudkov, A T]]

[[Category: Hughes, D]]

[[Category: Kristensen, O]]

[[Category: Laurberg, M]]

[[Category: Liljas, A]]

[[Category: Martemyanov, K]]

[[Category: Nagaev, I]]

[[Category: Visible domain iii]]