1r5b

<table><tr><td colspan='2'>[[1r5b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R5B FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r5n|1r5n]], [[1r5o|1r5o]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUP35, SPCC584.04 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=1r5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5b OCA], [http://pdbe.org/1r5b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r5b RCSB], [http://www.ebi.ac.uk/pdbsum/1r5b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5b ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ERF3_SCHPO ERF3_SCHPO]] Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides.

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== Publication Abstract from PubMed ==

Translation termination in eukaryotes is governed by two interacting release factors, eRF1 and eRF3. The crystal structure of the eEF1alpha-like region of eRF3 from S. pombe determined in three states (free protein, GDP-, and GTP-bound forms) reveals an overall structure that is similar to EF-Tu, although with quite different domain arrangements. In contrast to EF-Tu, GDP/GTP binding to eRF3c does not induce dramatic conformational changes, and Mg(2+) is not required for GDP binding to eRF3c. Mg(2+) at higher concentration accelerates GDP release, suggesting a novel mechanism for nucleotide exchange on eRF3 from that of other GTPases. Mapping sequence conservation onto the molecular surface, combined with mutagenesis analysis, identified the eRF1 binding region, and revealed an essential function for the C terminus of eRF3. The N-terminal extension, rich in acidic amino acids, blocks the proposed eRF1 binding site, potentially regulating eRF1 binding to eRF3 in a competitive manner.

Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe.,Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H Mol Cell. 2004 Apr 23;14(2):233-45. PMID:15099522<ref>PMID:15099522</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 1r5b" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cbs 356]]

[[Category: Kong, C]]

[[Category: Song, H]]

[[Category: Gtpase]]

[[Category: Translation termination]]