View source for 3qmn


==Crystal Structure of 4'-Phosphopantetheinyl Transferase AcpS from Vibrio cholerae O1 biovar eltor==
<StructureSection load='3qmn' size='340' side='right'caption='[[3qmn]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qmn]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibch Vibch]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ota 3ota] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h88 3h88]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QMN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3h88|3h88]], [[3ota|3ota]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acpS, VC_2457 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Holo-[acyl-carrier-protein]_synthase Holo-[acyl-carrier-protein] synthase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3qmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmn OCA], [https://pdbe.org/3qmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qmn RCSB], [https://www.ebi.ac.uk/pdbsum/3qmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmn ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ACPS_VIBCH ACPS_VIBCH]] Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.[HAMAP-Rule:MF_00101] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Some bacterial type II fatty-acid synthesis (FAS II) enzymes have been shown to be important candidates for drug discovery. The scientific and medical quest for new FAS II protein targets continues to stimulate research in this field. One of the possible additional candidates is the acyl-carrier-protein synthase (AcpS) enzyme. Its holo form post-translationally modifies the apo form of an acyl carrier protein (ACP), which assures the constant delivery of thioester intermediates to the discrete enzymes of FAS II. At the Center for Structural Genomics of Infectious Diseases (CSGID), AcpSs from Staphylococcus aureus (AcpS(SA)), Vibrio cholerae (AcpS(VC)) and Bacillus anthracis (AcpS(BA)) have been structurally characterized in their apo, holo and product-bound forms, respectively. The structure of AcpS(BA) is emphasized because of the two 3',5'-adenosine diphosphate (3',5'-ADP) product molecules that are found in each of the three coenzyme A (CoA) binding sites of the trimeric protein. One 3',5'-ADP is bound as the 3',5'-ADP part of CoA in the known structures of the CoA-AcpS and 3',5'-ADP-AcpS binary complexes. The position of the second 3',5'-ADP has never been described before. It is in close proximity to the first 3',5'-ADP and the ACP-binding site. The coordination of two ADPs in AcpS(BA) may possibly be exploited for the design of AcpS inhibitors that can block binding of both CoA and ACP.

Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.,Halavaty AS, Kim Y, Minasov G, Shuvalova L, Dubrovska I, Winsor J, Zhou M, Onopriyenko O, Skarina T, Papazisi L, Kwon K, Peterson SN, Joachimiak A, Savchenko A, Anderson WF Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1359-70. Epub 2012 Sep, 13. PMID:22993090<ref>PMID:22993090</ref>

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

==See Also==
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibch]]
[[Category: Anderson, W F]]
[[Category: Structural genomic]]
[[Category: Halavaty, A S]]
[[Category: Joachimiak, A]]
[[Category: Kim, Y]]
[[Category: Kwon, K]]
[[Category: Zhou, M]]
[[Category: Acyl carrier protein]]
[[Category: Alpha-beta sandwich]]
[[Category: Csgid]]
[[Category: Cytosol]]
[[Category: Transferase]]