Abstract
The first structure of the catalytic domain of RpfC (Rv1884), one of the resuscitation-promoting factors (RPFs) from Mycobacterium tuberculosis, is reported. The structure was solved using molecular replacement once the space group had been correctly identified as twinned P21 rather than the apparent C2221 by searching for anomalous scattering sites in P1. The structure displays a very high degree of structural conservation with the previously published structures of the catalytic domains of RpfB (Rv1009) and RpfE (Rv2450). This structural conservation highlights the importance of the versatile domain composition of the RPF family.
Highlights
Resuscitation-promoting factors (RPFs) have attracted much interest since their discovery in the late 1990s
We describe the X-ray structure of the RpfC catalytic domain
The sequence coding for the catalytic domain of RpfC was cloned into the NdeI and NheI sites of the pET15-TEV plasmid to generate a recombinant protein containing a six-histidine tag at the N-terminus cleavable by Tobacco Etch Virus (TEV) protease (Cohen-Gonsaud, Barthe et al, 2004)
Summary
Resuscitation-promoting factors (RPFs) have attracted much interest since their discovery in the late 1990s. These proteins resuscitate bacteria that have entered a dormant state, allowing them to proliferate normally. The factor was identified as a protein and named resuscitation-promoting factor. In this same seminal study, corresponding genes in other GC-rich Gram-positive bacteria, most notably in Mycobacterium tuberculosis, were identified. The resuscitating function was later confirmed in M. tuberculosis (Mukamolova et al, 2002). This is an important finding, as one third of the human population is latently infected with M. tuberculosis in a dormant form. This represents a large population reservoir for reactivation of tuberculosis and a potential novel therapeutic avenue for treating tuberculosis
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