3HST
N-Terminal RNASE H domain of rv2228c from mycobacterium tuberculosis as a fusion protein with maltose binding protein
Summary for 3HST
| Entry DOI | 10.2210/pdb3hst/pdb |
| Related PRD ID | PRD_900009 |
| Descriptor | Maltose-binding periplasmic protein, Protein Rv2228c/MT2287, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | ribonuclease h1, rv2228c n-terminal domain, mycobacterium, tuberculosis, fusion protein, maltose binding protein, hydrolase |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 4 |
| Total formula weight | 116516.60 |
| Authors | Watkins, H.A.,Baker, E.N. (deposition date: 2009-06-10, release date: 2010-04-28, Last modification date: 2024-02-21) |
| Primary citation | Watkins, H.A.,Baker, E.N. Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis. J.Bacteriol., 192:2878-2886, 2010 Cited by PubMed Abstract: The open reading frame Rv2228c from Mycobacterium tuberculosis is predicted to encode a protein composed of two domains, each with individual functions, annotated through sequence similarity searches. The N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with alpha-ribazole phosphatase (CobC). The N-terminal domain of Rv2228c (Rv2228c/N) and the full-length protein were expressed as fusions with maltose binding protein (MBP). Rv2228c/N was shown to have RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. The full-length protein was shown to have additional CobC activity. The crystal structure of the MBP-Rv2228c/N fusion protein was solved by molecular replacement and refined at 2.25-A resolution (R = 0.182; R(free) = 0.238). The protein is monomeric in solution but associates in the crystal to form a dimer. The Rv2228c/N domain has the classic RNase H fold and catalytic machinery but lacks several surface features that play important roles in the cleavage of RNA/DNA hybrids by other RNases H. The absence of either the basic protrusion of some RNases H or the hybrid binding domain of others appears to be compensated by the C-terminal CobC domain in full-length Rv2228c. The double-stranded-RNase activity of Rv2228c/N contrasts with classical RNases H and is attributed to the absence in Rv2228c/N of a key phosphate binding pocket. PubMed: 20363939DOI: 10.1128/JB.01615-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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