5o9v: Difference between revisions

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New page: '''Unreleased structure''' The entry 5o9v is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 5o9v is ON HOLD  until Paper Publication
==HsNMT1 in complex with CoA and Myristoylated-GGCFSKPK octapeptide==
<StructureSection load='5o9v' size='340' side='right'caption='[[5o9v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5o9v]] is a 4 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=5O9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O9V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.201&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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=5o9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9v OCA], [https://pdbe.org/5o9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o9v RCSB], [https://www.ebi.ac.uk/pdbsum/5o9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NMT1_HUMAN NMT1_HUMAN] Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An organism's entire protein modification repertoire has yet to be comprehensively mapped. N-myristoylation (MYR) is a crucial eukaryotic N-terminal protein modification. Here we mapped complete Homo sapiens and Arabidopsis thaliana myristoylomes. The crystal structures of human modifier NMT1 complexed with reactive and nonreactive target-mimicking peptide ligands revealed unexpected binding clefts and a modifier recognition pattern. This information allowed integrated mapping of myristoylomes using peptide macroarrays, dedicated prediction algorithms, and in vivo mass spectrometry. Global MYR profiling at the genomic scale identified over a thousand novel, heterogeneous targets in both organisms. Surprisingly, MYR involved a non-negligible set of overlapping targets with N-acetylation, and the sequence signature marks for a third proximal acylation-S-palmitoylation-were genomically imprinted, allowing recognition of sequences exhibiting both acylations. Together, the data extend the N-end rule concept for Gly-starting proteins to subcellular compartmentalization and reveal the main neighbors influencing protein modification profiles and consequent cell fate.


Authors:  
Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern.,Castrec B, Dian C, Ciccone S, Ebert CL, Bienvenut WV, Le Caer JP, Steyaert JM, Giglione C, Meinnel T Nat Chem Biol. 2018 Jun 11. pii: 10.1038/s41589-018-0077-5. doi:, 10.1038/s41589-018-0077-5. PMID:29892081<ref>PMID:29892081</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5o9v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dian C]]
[[Category: Giglione C]]
[[Category: Meinnel T]]
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