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| | ==HsNMT1 in complex with CoA and Myristoylated-GGCFSKPK octapeptide== | | ==HsNMT1 in complex with CoA and Myristoylated-GGCFSKPK octapeptide== |
| - | <StructureSection load='5o9v' size='340' side='right' caption='[[5o9v]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='5o9v' size='340' side='right'caption='[[5o9v]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5o9v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O9V FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.201Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMT1, NMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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'>[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> |
| - | <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=5o9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9v OCA], [http://pdbe.org/5o9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o9v RCSB], [http://www.ebi.ac.uk/pdbsum/5o9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. [[http://www.uniprot.org/uniprot/AIFM3_HUMAN AIFM3_HUMAN]] Induces apoptosis through a caspase dependent pathway. Reduces mitochondrial membrane potential.<ref>PMID:15764604</ref> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycylpeptide N-tetradecanoyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Dian, C]] | + | [[Category: Dian C]] |
| - | [[Category: Giglione, C]] | + | [[Category: Giglione C]] |
| - | [[Category: Meinnel, T]] | + | [[Category: Meinnel T]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Coa]]
| + | |
| - | [[Category: Glycylpeptide n-tetradecanoyltransferase 1 n-myristoyltransferase 1]]
| + | |
| - | [[Category: Gnat]]
| + | |
| - | [[Category: Myr-coa]]
| + | |
| - | [[Category: Myr-peptide]]
| + | |
| - | [[Category: Myristoyl]]
| + | |
| - | [[Category: N-myristoyltransferase type1]]
| + | |
| - | [[Category: Nmt]]
| + | |
| - | [[Category: Nmt1]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NMT1_HUMAN Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Castrec B, Dian C, Ciccone S, Ebert CL, Bienvenut WV, Le Caer JP, Steyaert JM, Giglione C, Meinnel T. Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern. Nat Chem Biol. 2018 Jun 11. pii: 10.1038/s41589-018-0077-5. doi:, 10.1038/s41589-018-0077-5. PMID:29892081 doi:http://dx.doi.org/10.1038/s41589-018-0077-5
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