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| | ==High-resolution structure of chorismate mutase from Corynebacterium glutamicum== | | ==High-resolution structure of chorismate mutase from Corynebacterium glutamicum== |
| - | <StructureSection load='5hub' size='340' side='right' caption='[[5hub]], [[Resolution|resolution]] 1.06Å' scene=''> | + | <StructureSection load='5hub' size='340' side='right'caption='[[5hub]], [[Resolution|resolution]] 1.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hub]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HUB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HUB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.06Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cgl0853 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=5hub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hub OCA], [https://pdbe.org/5hub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hub RCSB], [https://www.ebi.ac.uk/pdbsum/5hub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hub ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hub OCA], [http://pdbe.org/5hub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hub RCSB], [http://www.ebi.ac.uk/pdbsum/5hub PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hub ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8NS29_CORGL Q8NS29_CORGL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5hub" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5hub" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[3D structures of chorismate mutase|3D structures of chorismate mutase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcus glutamicus kinoshita et al. 1958]] | + | [[Category: Corynebacterium glutamicum]] |
| - | [[Category: Chorismate mutase]] | + | [[Category: Large Structures]] |
| - | [[Category: Burschowsky, D]] | + | [[Category: Burschowsky D]] |
| - | [[Category: Heim, J B]] | + | [[Category: Heim JB]] |
| - | [[Category: Krengel, U]] | + | [[Category: Krengel U]] |
| - | [[Category: Thorbjoernsrud, H V]] | + | [[Category: Thorbjoernsrud HV]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Pericyclic reaction]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| Structural highlights
Function
Q8NS29_CORGL
Publication Abstract from PubMed
Corynebacterium glutamicum is widely used for the industrial production of amino acids, nucleotides, and vitamins. The shikimate pathway enzymes DAHP synthase (CgDS; Cg2391) and chorismate mutase (CgCM; Cgl0853) play a key role for the biosynthesis of aromatic compounds. Here we show that CgCM requires the formation of a complex with CgDS to achieve full activity, and that both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Kinetic analysis showed that Phe and Tyr inhibit CgCM activity by inter-enzyme allostery, whereas Trp binding to CgDS strongly activates CgCM. Mechanistic insights were gained from crystal structures of the CgCM homodimer, tetrameric CgDS, and the heterooctameric CgCM-CgDS complex, refined to 1.1, 2.5, and 2.2 A resolution, respectively. Structural details from the allosteric binding sites reveal that DAHP synthase is recruited as the dominant regulatory platform to control the shikimate pathway, similar to the corresponding enzyme complex from Mycobacterium tuberculosis.
Inter-enzyme allosteric regulation of chorismate mutase in Corynebacterium glutamicum: Structural basis of feedback activation by Trp.,Burschowsky D, Thorbjornsrud HV, Heim JB, Fahrig-Kamarauskaite J, Wurth-Roderer K, Kast P, Krengel U Biochemistry. 2017 Nov 27. doi: 10.1021/acs.biochem.7b01018. PMID:29178787[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Burschowsky D, Thorbjornsrud HV, Heim JB, Fahrig-Kamarauskaite J, Wurth-Roderer K, Kast P, Krengel U. Inter-enzyme allosteric regulation of chorismate mutase in Corynebacterium glutamicum: Structural basis of feedback activation by Trp. Biochemistry. 2017 Nov 27. doi: 10.1021/acs.biochem.7b01018. PMID:29178787 doi:http://dx.doi.org/10.1021/acs.biochem.7b01018
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