1rq0

<table><tr><td colspan='2'>[[1rq0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RQ0 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRFA, TM1363 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rq0 OCA], [http://pdbe.org/1rq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rq0 RCSB], [http://www.ebi.ac.uk/pdbsum/1rq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rq0 ProSAT], [http://www.topsan.org/Proteins/BSGC/1rq0 TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/RF1_THEMA RF1_THEMA]] Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA (By similarity).

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== Publication Abstract from PubMed ==

We have determined the crystal structure of peptide chain release factor 1 (RF1) from Thermotoga maritima (gi 4981173) at 2.65 Angstrom resolution by selenomethionine single-wavelength anomalous dispersion (SAD) techniques. RF1 is a protein that recognizes stop codons and promotes the release of a nascent polypeptide from tRNA on the ribosome. Selenomethionine-labeled RF1 crystallized in space group P2(1) with three monomers per asymmetric unit. It has approximate dimensions of 75 Angstrom x 70 Angstrom x 45 Angstrom and is composed of four domains. The overall fold of each RF1 domain shows almost the same topology with Escherichia coli RF2, except that the RF1 N-terminal domain is shorter and the C-terminal domain is longer than that of RF2. The N-terminal domain of RF1 indicates a rigid-body movement relative to that of RF2 with an angle of approximately 90 degrees. Including these features, RF1 has a tripeptide anticodon PVT motif instead of the SPF motif of RF2, which confers the specificity towards the stop codons. The analyses of three molecules in the asymmetric unit and comparison with RF2 revealed the presence of dynamic movement of domains I and III, which are anchored to the central domain by hinge loops. The crystal structure of RF1 elucidates the intrinsic property of this family of having large domain movements for proper function with the ribosome.

Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome.,Shin DH, Brandsen J, Jancarik J, Yokota H, Kim R, Kim SH J Mol Biol. 2004 Jul 30;341(1):227-39. PMID:15312775<ref>PMID:15312775</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 1rq0" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: Structural genomic]]

[[Category: Brandsen, J]]

[[Category: Jancarik, J]]

[[Category: Kim, R]]

[[Category: Kim, S H]]

[[Category: Shin, D H]]

[[Category: Yokota, H]]

[[Category: Ribosome]]