View source for 9qlp


==NMT1-NAC bound human RNC with full length ARF1 - State 2==
<StructureSection load='9qlp' size='340' side='right'caption='[[9qlp]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9qlp]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9QLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QLP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G3D:GUANOSINE-3-MONOPHOSPHATE-5-DIPHOSPHATE'>G3D</scene>, <scene name='pdbligand=LYO:4-HYDROXY-LYSINE'>LYO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9qlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qlp OCA], [https://pdbe.org/9qlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qlp RCSB], [https://www.ebi.ac.uk/pdbsum/9qlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qlp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RS13_HUMAN RS13_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co-translationally by N-myristoyltransferases (NMTs) which have been identified as promising drug targets. However, its molecular basis in the context of the translating ribosome is not known. Here, we reveal the structural basis for co-translational N-myristoylation by NMT1 on the human ribosome by cryo-electron microscopy (cryo-EM). We show that NMT1 binds near the peptide tunnel exit and interacts with the nascent polypeptide-associated complex (NAC). Unlike other multi-enzyme complexes that act simultaneously, we find that methionine excision by methionine aminopeptidases and N-myristoylation occur sequentially via consecutive binding to the ribosome. Furthermore, our data suggest that NMT1 remains associated with elongating nascent chains, indicating a co-translational chaperone-like function in partnership with NAC. These insights provide a molecular foundation for the understanding of the co-translational N-myristoylation mechanism in humans.

Structural basis of co-translational N-myristoylation in humans.,Denk T, Monassa P, Musial J, Berninghausen O, Beatrix B, Giglione C, Meinnel T, Beckmann R Nat Commun. 2026 Jan 23;17(1):1191. doi: 10.1038/s41467-025-67962-4. PMID:41577716<ref>PMID:41577716</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9qlp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Beckmann R]]
[[Category: Berninghausen O]]
[[Category: Denk T]]