6qrm: Difference between revisions
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New page: '''Unreleased structure''' The entry 6qrm is ON HOLD Authors: Dian, C., Riviere, F.B., Giglione, C., Meinnel, T. Description: HsNMT1 in complex with both MyrCoA and GNCFSKRRAA substrat... |
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==HsNMT1 in complex with both MyrCoA and GNCFSKRRAA substrates== | |||
<StructureSection load='6qrm' size='340' side='right'caption='[[6qrm]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qrm]] 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=6QRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QRM 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]] 2.3Å</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=MYA:TETRADECANOYL-COA'>MYA</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=6qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qrm OCA], [https://pdbe.org/6qrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qrm RCSB], [https://www.ebi.ac.uk/pdbsum/6qrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qrm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AIFM3_HUMAN AIFM3_HUMAN] Induces apoptosis through a caspase dependent pathway. Reduces mitochondrial membrane potential.<ref>PMID:15764604</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The promising drug target N-myristoyltransferase (NMT) catalyses an essential protein modification thought to occur exclusively at N-terminal glycines (Gly). Here, we present high-resolution human NMT1 structures co-crystallised with reactive cognate lipid and peptide substrates, revealing high-resolution snapshots of the entire catalytic mechanism from the initial to final reaction states. Structural comparisons, together with biochemical analysis, provide unforeseen details about how NMT1 reaches a catalytically competent conformation in which the reactive groups are brought into close proximity to enable catalysis. We demonstrate that this mechanism further supports efficient and unprecedented myristoylation of an N-terminal lysine side chain, providing evidence that NMT acts both as N-terminal-lysine and glycine myristoyltransferase. | |||
High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation.,Dian C, Perez-Dorado I, Riviere F, Asensio T, Legrand P, Ritzefeld M, Shen M, Cota E, Meinnel T, Tate EW, Giglione C Nat Commun. 2020 Feb 28;11(1):1132. doi: 10.1038/s41467-020-14847-3. PMID:32111831<ref>PMID:32111831</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6qrm" style="background-color:#fffaf0;"></div> | ||
[[Category: Dian | == References == | ||
[[Category: Giglione | <references/> | ||
[[Category: Riviere | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Asensio T]] | |||
[[Category: Dian C]] | |||
[[Category: Giglione C]] | |||
[[Category: Meinnel T]] | |||
[[Category: Riviere FB]] | |||
Latest revision as of 05:41, 21 November 2024
HsNMT1 in complex with both MyrCoA and GNCFSKRRAA substrates
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