Open AccessPurification, crystallization and preliminary X‐ray studies of MbtN (Rv1346) from Mycobacterium tuberculosis
Author(s) -
Chai AiFen,
Johnston Jodie M.,
Bunker Richard D.,
Bulloch Esther M. M.,
Evans Genevieve L.,
Lott J. Shaun,
Baker Edward N.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113027000
Subject(s) - moiety , crystallization , double bond , chemistry , acyl group , dehydrogenation , stereochemistry , fatty acid , enzyme , crystallography , biochemistry , group (periodic table) , organic chemistry , catalysis
In Mycobacterium tuberculosis , the protein MbtN (Rv1346) catalyzes the formation of a double bond in the fatty‐acyl moiety of the siderophore mycobactin, which is used by this organism to acquire essential iron. MbtN is homologous to acyl‐CoA dehydrogenases, whose general role is to catalyze the α,β‐dehydrogenation of fatty‐acyl‐CoA conjugates. Mycobactins, however, contain a long unsaturated fatty‐acid chain with an unusual cis double bond conjugated to the carbonyl group of the mycobactin core. To characterize the role of MbtN in the dehydrogenation of this fatty‐acyl moiety, the enzyme has been expressed, purified and crystallized. The crystals diffracted to 2.3 Å resolution at a synchrotron source and were found to belong to the hexagonal space group H 3 2 , with unit‐cell parameters a = b = 139.10, c = 253.09 Å, α = β = 90, γ = 120°.