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| | <StructureSection load='2w19' size='340' side='right'caption='[[2w19]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='2w19' size='340' side='right'caption='[[2w19]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w19]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W19 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2w19]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W19 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vkl|2vkl]], [[2b7o|2b7o]], [[2w1a|2w1a]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-deoxy-7-phosphoheptulonate_synthase 3-deoxy-7-phosphoheptulonate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.54 2.5.1.54] </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=2w19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w19 OCA], [https://pdbe.org/2w19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w19 RCSB], [https://www.ebi.ac.uk/pdbsum/2w19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w19 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=2w19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w19 OCA], [https://pdbe.org/2w19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w19 RCSB], [https://www.ebi.ac.uk/pdbsum/2w19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w19 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AROG_MYCTU AROG_MYCTU] Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate.<ref>PMID:16288916</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[DAHP synthase 3D structures|DAHP synthase 3D structures]] | | *[[DAHP synthase 3D structures|DAHP synthase 3D structures]] |
| | + | *[[3D structures of chorismate mutase|3D structures of chorismate mutase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-deoxy-7-phosphoheptulonate synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Codoni, G]] | + | [[Category: Codoni G]] |
| - | [[Category: Gamper, M]] | + | [[Category: Gamper M]] |
| - | [[Category: Kast, P]] | + | [[Category: Kast P]] |
| - | [[Category: Krengel, U]] | + | [[Category: Krengel U]] |
| - | [[Category: Okvist, M]] | + | [[Category: Okvist M]] |
| - | [[Category: Roderer, K]] | + | [[Category: Roderer K]] |
| - | [[Category: Sasso, S]] | + | [[Category: Sasso S]] |
| - | [[Category: Aromatic amino acid biosynthesis]]
| + | |
| - | [[Category: Complex formation]]
| + | |
| - | [[Category: Drug target]]
| + | |
| - | [[Category: Enzyme activation]]
| + | |
| - | [[Category: Enzyme catalysis]]
| + | |
| - | [[Category: Feedback regulation]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Multi-enzyme complex]]
| + | |
| - | [[Category: Mycobacterium tuberculosis rv0948c]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase isomerase complex]]
| + | |
| - | [[Category: Transferase-isomerase complex]]
| + | |
| Structural highlights
Function
AROG_MYCTU Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate.[1]
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
Chorismate mutase catalyzes a key step in the shikimate biosynthetic pathway towards phenylalanine and tyrosine. Curiously, the intracellular chorismate mutase of Mycobacterium tuberculosis (MtCM; Rv0948c) has poor activity and lacks prominent active-site residues. However, its catalytic efficiency increases >100-fold on addition of DAHP synthase (MtDS; Rv2178c), another shikimate-pathway enzyme. The 2.35 A crystal structure of the MtCM-MtDS complex bound to a transition-state analogue shows a central core formed by four MtDS subunits sandwiched between two MtCM dimers. Structural comparisons imply catalytic activation to be a consequence of the repositioning of MtCM active-site residues on binding to MtDS. The mutagenesis of the C-terminal extrusion of MtCM establishes conserved residues as part of the activation machinery. The chorismate-mutase activity of the complex, but not of MtCM alone, is inhibited synergistically by phenylalanine and tyrosine. The complex formation thus endows the shikimate pathway of M. tuberculosis with an important regulatory feature. Experimental evidence suggests that such non-covalent enzyme complexes comprising an AroQ(delta) subclass chorismate mutase like MtCM are abundant in the bacterial order Actinomycetales.
Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.,Sasso S, Okvist M, Roderer K, Gamper M, Codoni G, Krengel U, Kast P EMBO J. 2009 Jul 22;28(14):2128-42. Epub 2009 Jun 25. PMID:19556970[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Webby CJ, Baker HM, Lott JS, Baker EN, Parker EJ. The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes. J Mol Biol. 2005 Dec 9;354(4):927-39. Epub 2005 Oct 21. PMID:16288916 doi:10.1016/j.jmb.2005.09.093
- ↑ Sasso S, Okvist M, Roderer K, Gamper M, Codoni G, Krengel U, Kast P. Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner. EMBO J. 2009 Jul 22;28(14):2128-42. Epub 2009 Jun 25. PMID:19556970 doi:10.1038/emboj.2009.165
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