1tr8

<table><tr><td colspan='2'>[[1tr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_2133 Dsm 2133]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TR8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TR8 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTH177 (amonoacids 19-117) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145263 DSM 2133])</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=1tr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tr8 OCA], [http://pdbe.org/1tr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1tr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tr8 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NAC_METTM NAC_METTM]] Contacts the emerging nascent chain on the ribosome.[HAMAP-Rule:MF_00814]

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== Publication Abstract from PubMed ==

Nascent polypeptide-associated complex (NAC) was identified in eukaryotes as the first cytosolic factor that contacts the nascent polypeptide chain emerging from the ribosome. NAC is highly conserved from yeast to humans. Mutations in NAC cause severe embryonically lethal phenotypes in mice, Drosophila, and Caenorhabditis elegans. NAC was suggested to protect the nascent chain from inappropriate early interactions with cytosolic factors. Eukaryotic NAC is a heterodimer with two subunits sharing substantial homology with each other. All sequenced archaebacterial genomes exhibit only one gene homologous to the NAC subunits. Here we present the first archaebacterial NAC homolog. It forms a homodimer, and as eukaryotic NAC it is associated with ribosomes and contacts the emerging nascent chain on the ribosome. We present the first crystal structure of a NAC protein revealing two structural features: (i) a novel unique protein fold that mediates dimerization of the complex, and (ii) a ubiquitin-associated domain that suggests a yet unidentified role for NAC in the cellular protein quality control system via the ubiquitination pathway. Based on the presented structure we propose a model for the eukaryotic heterodimeric NAC domain.

The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.,Spreter T, Pech M, Beatrix B J Biol Chem. 2005 Apr 22;280(16):15849-54. Epub 2005 Jan 22. PMID:15665334<ref>PMID:15665334</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 1tr8" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Dsm 2133]]

[[Category: Beatrix, B]]

[[Category: Pech, M]]

[[Category: Spreter, T]]

[[Category: Chaperone]]

[[Category: Ubiquitin]]