View source for 4qbj


==Crystal structure of N-myristoyl transferase from Aspergillus fumigatus complexed with a synthetic inhibitor==
<StructureSection load='4qbj' size='340' side='right'caption='[[4qbj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qbj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QBJ 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2XQ:3-[[3-METHYL-2-[[2,3,4-TRIS(FLUORANYL)PHENOXY]METHYL]-1-BENZOFURAN-4-YL]OXY]-N-(PYRIDIN-3-YLMETHYL)PROPAN-1-AMINE'>2XQ</scene>, <scene name='pdbligand=NHM:S-(2-OXO)PENTADECYLCOA'>NHM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4qbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qbj OCA], [https://pdbe.org/4qbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qbj RCSB], [https://www.ebi.ac.uk/pdbsum/4qbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qbj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NMT_ASPFU NMT_ASPFU] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-Myristoyltransferase (NMT) is an enzyme which translocates the 14-carbon saturated fatty acid myristate from myristoyl-CoA to the N-terminal glycine of substrate peptides. This myristoylation process is involved in protein modification in various eukaryotes, including animals and fungi. Furthermore, this enzyme has been shown to be essential to the growth of various species, such as Saccharomyces cerevisiae, which indicates that NMT is an attractive target for the development of a novel antifungal drug. In this study, the crystal structure of a ternary complex of NMT from Aspergillus fumigatus with S-(2-oxo)pentadecyl-CoA, a myristoyl-CoA analogue cofactor, and a synthetic inhibitor is reported at a resolution of 2.1 A. The results advance the understanding of the specificity of NMT inhibitors and provide valuable information for structure-based drug design.

Structure of N-myristoyltransferase from Aspergillus fumigatus.,Shimada T, Suzuki M, Katakura SI Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):754-61. doi:, 10.1107/S1399004715000401. Epub 2015 Mar 26. PMID:25849386<ref>PMID:25849386</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qbj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus fumigatus Af293]]
[[Category: Large Structures]]
[[Category: Shimada T]]
[[Category: Suzuki M]]