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3nfd

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Current revision (09:59, 14 February 2024) (edit) (undo)
 
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<StructureSection load='3nfd' size='340' side='right'caption='[[3nfd]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
<StructureSection load='3nfd' size='340' side='right'caption='[[3nfd]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3nfd]] is a 6 chain structure with sequence from [https://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=3NFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NFD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3nfd]] is a 6 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=3NFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NFD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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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]] 1.89&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ne9|3ne9]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1697 "Bacterium ammoniagenes" Cooke and Keith 1927])</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=3nfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nfd OCA], [https://pdbe.org/3nfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nfd RCSB], [https://www.ebi.ac.uk/pdbsum/3nfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nfd ProSAT]</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=3nfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nfd OCA], [https://pdbe.org/3nfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nfd RCSB], [https://www.ebi.ac.uk/pdbsum/3nfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nfd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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]
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3nfd" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacterium ammoniagenes cooke and keith 1927]]
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[[Category: Corynebacterium ammoniagenes]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gokulan, K]]
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[[Category: Gokulan K]]
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[[Category: Acyl carrier protein]]
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[[Category: Acyl carrier protein synthase]]
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[[Category: Fatty acid synthase]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Transferase]]
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Current revision

Chronobacterium ammoniagenes ACPS-CoA complex

PDB ID 3nfd

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