2qj3

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(New page: 200px<br /><applet load="2qj3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qj3, resolution 3.00&Aring;" /> '''Mycobacterium tuberc...)
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[[Image:2qj3.jpg|left|200px]]<br /><applet load="2qj3" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2qj3, resolution 3.00&Aring;" />
 
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'''Mycobacterium tuberculosis FabD'''<br />
 
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==Overview==
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==Mycobacterium tuberculosis FabD==
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Mycobacteria display a unique and unusual cell-wall architecture, central, to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan, core (mAGP). The biosynthesis of mycolic acids, which form the outermost, layer of the mAGP core, involves malonyl-CoA:acyl carrier protein, transacylase (MCAT). This essential enzyme catalyses the transfer of, malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these, two-carbon units into the chain-elongation cycle of the type II fatty-acid, synthase. The crystal structure of M. tuberculosis mtFabD, the, mycobacterial MCAT, has been determined to 3.0 A resolution by, multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+, ions bound to the 20-residue N-terminal affinity tag, which packed between, the two independent copies of mtFabD.
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<StructureSection load='2qj3' size='340' side='right'caption='[[2qj3]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2qj3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QJ3 FirstGlance]. <br>
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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]] 3&#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=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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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=2qj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qj3 OCA], [https://pdbe.org/2qj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qj3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qj3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABD_MYCTU FABD_MYCTU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/2qj3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2qj3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.
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==About this Structure==
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Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).,Ghadbane H, Brown AK, Kremer L, Besra GS, Futterer K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):831-5. Epub 2007 Sep 19. PMID:17909282<ref>PMID:17909282</ref>
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2QJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJ3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)., Ghadbane H, Brown AK, Kremer L, Besra GS, Futterer K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):831-5. Epub 2007 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17909282 17909282]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 2qj3" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
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<references/>
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[[Category: Besra, G.S.]]
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__TOC__
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[[Category: Brown, A.K.]]
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</StructureSection>
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[[Category: Futterer, K.]]
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[[Category: Large Structures]]
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[[Category: Ghadbane, H.]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Kremer, L.]]
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[[Category: Besra GS]]
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[[Category: NI]]
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[[Category: Brown AK]]
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[[Category: fatty acid synthase ]]
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[[Category: Futterer K]]
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[[Category: malonyl-coa]]
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[[Category: Ghadbane H]]
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[[Category: mycolic acids]]
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[[Category: Kremer L]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:20:21 2008''
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Current revision

Mycobacterium tuberculosis FabD

PDB ID 2qj3

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