1nmt

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[[Image:1nmt.jpg|left|200px]]
 
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==N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A==
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The line below this paragraph, containing "STRUCTURE_1nmt", creates the "Structure Box" on the page.
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<StructureSection load='1nmt' size='340' side='right'caption='[[1nmt]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1nmt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NMT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_1nmt| PDB=1nmt | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmt OCA], [https://pdbe.org/1nmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nmt RCSB], [https://www.ebi.ac.uk/pdbsum/1nmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmt ProSAT]</span></td></tr>
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</table>
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'''N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A'''
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== Function ==
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[https://www.uniprot.org/uniprot/NMT_CANAL NMT_CANAL] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.<ref>PMID:1569105</ref> <ref>PMID:8300631</ref> <ref>PMID:9115247</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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N-myristoyl transferase (NMT) catalyzes the transfer of the fatty acid myristate from myristoyl-CoA to the N-terminal glycine of substrate proteins, and is found only in eukaryotic cells. The enzyme in this study is the 451 amino acid protein produced by Candida albicans, a yeast responsible for the majority of systemic infections in immuno-compromised humans. NMT activity is essential for vegetative growth, and the structure was determined in order to assist in the discovery of a selective inhibitor of NMT which could be developed as an anti-fungal drug. NMT has no sequence homology with other protein sequences and has a novel alpha/beta fold which shows internal two-fold symmetry, which may be a result of gene duplication. On one face of the protein there is a long, curved, relatively uncharged groove, at the center of which is a deep pocket. The pocket floor is negatively charged due to the vicinity of the C-terminal carboxylate and a nearby conserved glutamic acid residue, which separates the pocket from a cavity. These observations, considered alongside the positions of residues whose mutation affects substrate binding and activity, suggest that the groove and pocket are the sites of substrate binding and the floor of the pocket is the catalytic center.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nmt_consurf.spt"</scriptWhenChecked>
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1NMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMT OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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Crystal structure of the anti-fungal target N-myristoyl transferase., Weston SA, Camble R, Colls J, Rosenbrock G, Taylor I, Egerton M, Tucker AD, Tunnicliffe A, Mistry A, Mancia F, de la Fortelle E, Irwin J, Bricogne G, Pauptit RA, Nat Struct Biol. 1998 Mar;5(3):213-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9501915 9501915]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nmt ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Candida albicans]]
[[Category: Candida albicans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Transferase]]
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[[Category: Pauptit RA]]
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[[Category: Pauptit, R A.]]
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[[Category: Weston SA]]
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[[Category: Weston, S A.]]
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[[Category: Acyltransferase]]
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[[Category: Antifungal target]]
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[[Category: Coa]]
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[[Category: Myristylation]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:43:25 2008''
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Current revision

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

PDB ID 1nmt

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