6sk3: Difference between revisions
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==C-terminal HsNMT1 deltaC3 truncation in complex with both MyrCoA and GNCFSKPR substrates== | |||
<StructureSection load='6sk3' size='340' side='right'caption='[[6sk3]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6sk3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SK3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SK3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MYA:TETRADECANOYL-COA'>MYA</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycylpeptide_N-tetradecanoyltransferase Glycylpeptide N-tetradecanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.97 2.3.1.97] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6sk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sk3 OCA], [http://pdbe.org/6sk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sk3 RCSB], [http://www.ebi.ac.uk/pdbsum/6sk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sk3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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 == | |||
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> | ||
<div class="pdbe-citations 6sk3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glycylpeptide N-tetradecanoyltransferase]] | |||
[[Category: Large Structures]] | |||
[[Category: Asensio, T]] | [[Category: Asensio, T]] | ||
[[Category: Dian, C]] | [[Category: Dian, C]] | ||
[[Category: Giglione, C]] | [[Category: Giglione, C]] | ||
[[Category: Riviere, F | [[Category: Meinnel, T]] | ||
[[Category: Riviere, F B]] | |||
[[Category: Acyltransferase]] | |||
[[Category: Gcn5-related n-acetyltransferase]] | |||
[[Category: Gnat]] | |||
[[Category: Myristoyltransferase type1]] | |||
[[Category: Nmt]] | |||
[[Category: Transferase]] | |||
Latest revision as of 12:51, 18 March 2020
C-terminal HsNMT1 deltaC3 truncation in complex with both MyrCoA and GNCFSKPR substratesC-terminal HsNMT1 deltaC3 truncation in complex with both MyrCoA and GNCFSKPR substrates
Structural highlights
Function[NMT1_HUMAN] Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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