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==Crystal structure of a Mycobacterium tuberculosis chorismate mutase optimized for high autonomous activity by directed evolution==
==Crystal structure of a Mycobacterium tuberculosis chorismate mutase optimized for high autonomous activity by directed evolution==
<StructureSection load='5mpv' size='340' side='right' caption='[[5mpv]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
<StructureSection load='5mpv' size='340' side='right'caption='[[5mpv]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5mpv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MPV FirstGlance]. <br>
<table><tr><td colspan='2'>[[5mpv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MPV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MPV FirstGlance]. <br>
</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>
</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mpv OCA], [http://pdbe.org/5mpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mpv RCSB], [http://www.ebi.ac.uk/pdbsum/5mpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mpv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mpv OCA], [http://pdbe.org/5mpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mpv RCSB], [http://www.ebi.ac.uk/pdbsum/5mpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mpv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</StructureSection>
</StructureSection>
[[Category: Chorismate mutase]]
[[Category: Chorismate mutase]]
[[Category: Large Structures]]
[[Category: Kamarauskaite, J]]
[[Category: Kamarauskaite, J]]
[[Category: Kast, P]]
[[Category: Kast, P]]

Revision as of 10:25, 19 August 2020

Crystal structure of a Mycobacterium tuberculosis chorismate mutase optimized for high autonomous activity by directed evolutionCrystal structure of a Mycobacterium tuberculosis chorismate mutase optimized for high autonomous activity by directed evolution

Structural highlights

5mpv is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Chorismate mutase, with EC number 5.4.99.5
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CHMU_MYCTU] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.[1] [2] [3]

References

  1. ↑ Prakash P, Aruna B, Sardesai AA, Hasnain SE. Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity. J Biol Chem. 2005 May 20;280(20):19641-8. Epub 2005 Feb 28. PMID:15737998 doi:10.1074/jbc.M413026200
  2. ↑ Kim SK, Reddy SK, Nelson BC, Robinson H, Reddy PT, Ladner JE. A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis. FEBS J. 2008 Oct;275(19):4824-35. Epub 2008 Aug 22. PMID:18727669 doi:10.1111/j.1742-4658.2008.06621.x
  3. ↑ 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

5mpv, resolution 1.49Å

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