5mpv

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

5mpv is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.49Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

↑ 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
↑ 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
↑ 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