View source for 3ne3


==Mycobacterium tuberculosis Acyl Carrier Protein Synthase Apo structure==
<StructureSection load='3ne3' size='340' side='right' caption='[[3ne3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ne3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NE3 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ne1|3ne1]], [[3ne9|3ne9]], [[3nfd|3nfd]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acpS, MT2599, MTV009.08c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Holo-[acyl-carrier-protein]_synthase Holo-[acyl-carrier-protein] synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.7 2.7.8.7] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ne3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne3 OCA], [http://pdbe.org/3ne3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ne3 RCSB], [http://www.ebi.ac.uk/pdbsum/3ne3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne3 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ACPS_MYCTU ACPS_MYCTU]] Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein (By similarity). 
== 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/ne/3ne3_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=3ne3 ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The crystal structures of acyl carrier protein synthase (AcpS) from Mycobacterium tuberculosis (Mtb) and Corynebacterium ammoniagenes determined at pH 5.3 and pH 6.5, respectively, are reported. Comparison of the Mtb apo-AcpS structure with the recently reported structure of the Mtb AcpS-ADP complex revealed that AcpS adopts two different conformations: the orthorhombic and trigonal space-group structures show structural differences in the alpha2 helix and in the conformation of the alpha3-alpha4 connecting loop, which is in a closed conformation. The apo-AcpS structure shows electron density for the entire model and was obtained at lower pH values (4.4-6.0). In contrast, at a higher pH value (6.5) AcpS undergoes significant conformational changes, resulting in disordered regions that show no electron density in the AcpS model. The solved structures also reveal that C. ammoniagenes AcpS undergoes structural rearrangement in two regions, similar to the recently reported Mtb AcpS-ADP complex structure. In vitro reconstitution experiments show that AcpS has a higher post-translational modification activity between pH 4.4 and 6.0 than at pH values above 6.5, where the activity drops owing to the change in conformation. The results show that apo-AcpS and AcpS-ADP adopt different conformations depending upon the pH conditions of the crystallization solution.

Mycobacterium tuberculosis acyl carrier protein synthase adopts two different pH-dependent structural conformations.,Gokulan K, Aggarwal A, Shipman L, Besra GS, Sacchettini JC Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):657-69. doi:, 10.1107/S0907444911020221. Epub 2011 Jun 11. PMID:21697604<ref>PMID:21697604</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ne3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gokulan, K]]
[[Category: XMTB, Mycobacterium Tuberculosis Structural Proteomics Project]]
[[Category: Acp]]
[[Category: Acyl carrier protein]]
[[Category: Acyl carrier protein synthase]]
[[Category: Fatty acid synthase]]
[[Category: Mycobacterium tuberculosis structural proteomics project]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Xmtb]]