A proposed carbon‐utilization and virulence protein A, CuvA (Rv1422), from Mycobacterium tuberculosis H37Rv: crystallization, X‐ray diffraction analysis and ligand binding

Mycobacterium tuberculosis possesses the ability to undergo physiological adaptations in order to persist during the prolonged course of infection despite the active immune response of the host and in order to overcome multiple environmental changes. Previous studies have proposed that M. tuberculosis CuvA (Rv1422; MtCuvA) might play a critical role in the adaptation of the bacterium to environmental changes, such as nutrient utilization and alteration of the growth rate. However, the detailed function of MtCuvA still remains unclear owing to a lack of structural information. To better understand its role in host adaptation, MtCuvA was purified to homogeneity and was crystallized for the first time using the hanging‐drop vapor‐diffusion method. The crystal of MtCuvA diffracted to a resolution of 2.1 Å and belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 47.27, b = 170.93, c = 178.10 Å. The calculated Matthews coefficient (VM) was 2.4 Å3 Da−1, with a solvent content of 48.02%, and thus four molecules appeared to be present in the asymmetric unit. Moreover, it is reported that MtCuvA can bind to the cell‐wall precursor components uridine diphosphate (UDP)‐glucose and UDP‐N‐acetylglucosamine. This study presents the crystallization, X‐ray diffraction analysis and ligand binding of CuvA (Rv1422) from M. tuberculosis H37Rv and reports that MtCuvA can bind to the cell‐wall precursor components uridine diphosphate (UDP)‐glucose and UDP‐N‐acetylglucosamine.