This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2qj3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Current revision (08:21, 25 June 2021) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2qj3.jpg|left|200px]]<br /><applet load="2qj3" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2qj3, resolution 3.00&Aring;" />
 
-
'''Mycobacterium tuberculosis FabD'''<br />
 
-
==Overview==
+
==Mycobacterium tuberculosis FabD==
-
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.
+
<StructureSection load='2qj3' size='340' side='right'caption='[[2qj3]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2qj3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. 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>
 +
</td></tr><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>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=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>
 +
</table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/2qj3_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
==About this Structure==
+
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>
-
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].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: Mycobacterium tuberculosis]]
+
<div class="pdbe-citations 2qj3" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
+
<references/>
-
[[Category: Besra, G.S.]]
+
__TOC__
-
[[Category: Brown, A.K.]]
+
</StructureSection>
-
[[Category: Futterer, K.]]
+
[[Category: Large Structures]]
-
[[Category: Ghadbane, H.]]
+
[[Category: Myctu]]
-
[[Category: Kremer, L.]]
+
[[Category: Besra, G S]]
-
[[Category: NI]]
+
[[Category: Brown, A K]]
-
[[Category: fatty acid synthase ]]
+
[[Category: Futterer, K]]
-
[[Category: malonyl-coa]]
+
[[Category: Ghadbane, H]]
-
[[Category: mycolic acids]]
+
[[Category: Kremer, L]]
-
[[Category: transferase]]
+
[[Category: Fatty acid synthase]]
-
 
+
[[Category: Malonyl-coa]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:20:21 2008''
+
[[Category: Mycolic acid]]
 +
[[Category: Transferase]]

Current revision

Mycobacterium tuberculosis FabD

PDB ID 2qj3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools