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| | <StructureSection load='3ne9' size='340' side='right'caption='[[3ne9]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3ne9' size='340' side='right'caption='[[3ne9]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ne9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_ammoniagenes"_cooke_and_keith_1927 "bacterium ammoniagenes" cooke and keith 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NE9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ne9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NE9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ne1|3ne1]], [[3ne3|3ne3]]</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=3ne9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne9 OCA], [https://pdbe.org/3ne9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ne9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ne9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne9 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACPS, PPT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1697 "Bacterium ammoniagenes" Cooke and Keith 1927])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ne9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne9 OCA], [http://pdbe.org/3ne9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ne9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ne9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/O31302_CORAM O31302_CORAM]] Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.[HAMAP-Rule:MF_00101][SAAS:SAAS00089007] | + | [https://www.uniprot.org/uniprot/O31302_CORAM O31302_CORAM] Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.[HAMAP-Rule:MF_00101][SAAS:SAAS00089007] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/3ne9_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/3ne9_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium ammoniagenes cooke and keith 1927]] | + | [[Category: Corynebacterium ammoniagenes]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gokulan, K]] | + | [[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]]
| + | |
| Structural highlights
Function
O31302_CORAM Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.[HAMAP-Rule:MF_00101][SAAS:SAAS00089007]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gokulan K, Aggarwal A, Shipman L, Besra GS, Sacchettini JC. Mycobacterium tuberculosis acyl carrier protein synthase adopts two different pH-dependent structural conformations. Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):657-69. doi:, 10.1107/S0907444911020221. Epub 2011 Jun 11. PMID:21697604 doi:10.1107/S0907444911020221
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