Mycobacterium tuberculosis universal stress protein Rv2623 interacts with the putative ATP binding cassette (ABC) transporter Rv1747 to regulate mycobacterial growth
Fig 3
The Rv2623 threonine residues.
(A) The solvent accessible surface (SAS) of threonine residues and the corresponding OH group in each monomer of the dimeric Rv2623 was calculated based on the crystal structure of the USP (PDB ID 3CIS) [6] using AREAIMOL program from CCP4 suite [35,36]. Among the 9 Thr residues, 5 have solvent accessible hydroxyl oxygen atoms (Shaded: T90, T103, T212, T237, T280). T90, T103, T212, and T237 also have a previously reported phosphorylation motif concerning the pT+3 residues (bracketed): pTXX(S) for T90, pTXX(D) for T103, pTXX(M) for T212, and pTXX(V) for T237 [24,32,33]. KAPP: kinase associated protein phosphatase of Arabidopsis thaliana [72]; KIAA: also known as KIAA0710/NFBD1 (nuclear factor BRCT domain 1) [73,74]; CDS-1: Checkpoint DNA synthesis protein kinase [75]; Y127_MYCTU: Cy1A11.16C [32], M. tuberculosis GarA [tuberculist.epfl.ch]. (B) The surface of the Rv2623 protein is displayed using PYMOL (www.pymol.org). The subunits A and B are colored in blue cyan and green respectively. The solvent accessible Threonine residues (T90, T103, T212, T237) are colored in yellow. (C) PYMOL display of a ribbon representation of an Rv2623 monomer based on previously solved structure [6] depicting the position of the four solvent accessible threonine residues with the corresponding pT+3 residues that have been shown to promote interaction with FHA domains [24,32,33]. The threonine and the pT+3 residues are labeled in yellow and cyan, respectively.