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<StructureSection load='3tfc' size='340' side='right'caption='[[3tfc]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3tfc' size='340' side='right'caption='[[3tfc]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tfc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3tfc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</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]] 1.95&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aroA, lmo1600 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene></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=3tfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfc OCA], [https://pdbe.org/3tfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfc RCSB], [https://www.ebi.ac.uk/pdbsum/3tfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfc 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=3tfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfc OCA], [https://pdbe.org/3tfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfc RCSB], [https://www.ebi.ac.uk/pdbsum/3tfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfc ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8Y6T2_LISMO Q8Y6T2_LISMO]
3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) catalyzes the first step in the biosynthesis of a number of aromatic metabolites. Likely because this reaction is situated at a pivotal biosynthetic gateway, several DAHPS classes distinguished by distinct mechanisms of allosteric regulation have independently evolved. One class of DAHPSs contains a regulatory domain with sequence homology to chorismate mutase-an enzyme further downstream of DAHPS that catalyzes the first committed step in tyrosine/phenylalanine biosynthesis-and is inhibited by chorismate mutase substrate (chorismate) and product (prephenate). Described in this work, structures of the Listeria monocytogenes chorismate/prephenate regulated DAHPS in complex with Mn(2+) and Mn(2+) + phosphoenolpyruvate reveal an unusual quaternary architecture: DAHPS domains assemble as a tetramer, from either side of which chorismate mutase-like (CML) regulatory domains asymmetrically emerge to form a pair of dimers. This domain organization suggests that chorismate/prephenate binding promotes a stable interaction between the discrete regulatory and catalytic domains and supports a mechanism of allosteric inhibition similar to tyrosine/phenylalanine control of a related DAHPS class. We argue that the structural similarity of chorismate mutase enzyme and CML regulatory domain provides a unique opportunity for the design of a multitarget antibacterial.
 
Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain.,Light SH, Halavaty AS, Minasov G, Shuvalova L, Anderson WF Protein Sci. 2012 Apr 13. doi: 10.1002/pro.2075. PMID:22505283<ref>PMID:22505283</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tfc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[DAHP synthase 3D structures|DAHP synthase 3D structures]]
*[[DAHP synthase 3D structures|DAHP synthase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lismo]]
[[Category: Listeria monocytogenes EGD-e]]
[[Category: Anderson, W F]]
[[Category: Anderson WF]]
[[Category: Structural genomic]]
[[Category: Halavaty AS]]
[[Category: Halavaty, A S]]
[[Category: Kwon K]]
[[Category: Kwon, K]]
[[Category: Light SH]]
[[Category: Light, S H]]
[[Category: Minasov G]]
[[Category: Minasov, G]]
[[Category: Shuvalova L]]
[[Category: Shuvalova, L]]
[[Category: Csgid]]
[[Category: Tim barrel]]
[[Category: Transferase-isomerase complex]]
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