2ntn: Difference between revisions

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{{Seed}}
[[Image:2ntn.png|left|200px]]


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==Crystal structure of MabA-C60V/G139A/S144L==
The line below this paragraph, containing "STRUCTURE_2ntn", creates the "Structure Box" on the page.
<StructureSection load='2ntn' size='340' side='right'caption='[[2ntn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2ntn]] 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=2NTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NTN FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=2ntn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ntn OCA], [https://pdbe.org/2ntn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ntn RCSB], [https://www.ebi.ac.uk/pdbsum/2ntn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ntn ProSAT]</span></td></tr>
{{STRUCTURE_2ntn|  PDB=2ntn  |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/MABA_MYCTU MABA_MYCTU] Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis (PubMed:11932442). Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle (PubMed:9802011, PubMed:11932442, PubMed:17059223, PubMed:18155153, PubMed:19685079). May preferentially metabolize long-chain substrates (C8-C20) (PubMed:11932442). Can use CoA derivatives as substrates in vitro (PubMed:9802011, PubMed:11932442, PubMed:17059223, PubMed:18155153).<ref>PMID:11932442</ref> <ref>PMID:17059223</ref> <ref>PMID:18155153</ref> <ref>PMID:19685079</ref> <ref>PMID:9802011</ref>
== 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/nt/2ntn_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=2ntn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The MabA protein from Mycobacterium tuberculosis is a validated drug target. Previous structural studies of this protein showed dynamic behaviour in the catalytic site and described motion between an open 'active' holo form (with NADP) and a closed 'inactive' apo form (without NADP). Here, a mutation (G139A) is reported that leads to complete protein inactivation and freezes the catalytic site into its closed form, even in the presence of the cofactor. This observation suggests a new way to develop anti-MabA drugs via protein stabilization of the 'inactive' form.


===Crystal structure of MabA-C60V/G139A/S144L===
Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.,Poncet-Montange G, Ducasse-Cabanot S, Quemard A, Labesse G, Cohen-Gonsaud M Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):923-5. Epub 2007, Jul 17. PMID:17642518<ref>PMID:17642518</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ntn" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17642518}}, adds the Publication Abstract to the page
*[[Beta-ketoacyl carrier protein reductase 3D structures|Beta-ketoacyl carrier protein reductase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17642518 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17642518}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2NTN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NTN OCA].
[[Category: Mycobacterium tuberculosis H37Rv]]
 
[[Category: Cohen-Gonsaud M]]
==Reference==
[[Category: Ducasse-Cabanot S]]
Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies., Poncet-Montange G, Ducasse-Cabanot S, Quemard A, Labesse G, Cohen-Gonsaud M, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):923-5. Epub 2007, Jul 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17642518 17642518]
[[Category: Labesse G]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Poncet-Montange G]]
[[Category: Single protein]]
[[Category: Quemard A]]
[[Category: Cohen-Gonsaud, M.]]
[[Category: Ducasse-Cabanot, S.]]
[[Category: Labesse, G.]]
[[Category: Poncet-Montange, G.]]
[[Category: Quemard, A.]]
[[Category: Beta-ketoacyl acp reductase]]
[[Category: Inactive]]
[[Category: Oxidoreductase]]
[[Category: Sdr]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:24:02 2008''

Latest revision as of 08:55, 25 October 2023

Crystal structure of MabA-C60V/G139A/S144L

2ntn, resolution 2.30Å

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