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4HVJ

Crystal structure of a putative uncharacterized protein from Mycobacterium tuberculosis in complex with AMP

Summary for 4HVJ
Entry DOI10.2210/pdb4hvj/pdb
Related4HEC
DescriptorPutative uncharacterized protein, ADENOSINE MONOPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsssgcid, mycobacterium tuberculosis, structural genomics, seattle structural genomics center for infectious disease, adenosine monophosphate, unknown function
Biological sourceMycobacterium tuberculosis
Total number of polymer chains2
Total formula weight44265.25
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-11-06, release date: 2012-11-28, Last modification date: 2023-09-20)
Primary citationAbendroth, J.,Ollodart, A.,Andrews, E.S.,Myler, P.J.,Staker, B.L.,Edwards, T.E.,Arcus, V.L.,Grundner, C.
Mycobacterium tuberculosis Rv2179c Protein Establishes a New Exoribonuclease Family with Broad Phylogenetic Distribution.
J.Biol.Chem., 289:2139-2147, 2014
Cited by
PubMed Abstract: Ribonucleases (RNases) maintain the cellular RNA pool by RNA processing and degradation. In many bacteria, including the human pathogen Mycobacterium tuberculosis (Mtb), the enzymes mediating several central RNA processing functions are still unknown. Here, we identify the hypothetical Mtb protein Rv2179c as a highly divergent exoribonuclease. Although the primary sequence of Rv2179c has no detectable similarity to any known RNase, the Rv2179c crystal structure reveals an RNase fold. Active site residues are equivalent to those in the DEDD family of RNases, and Rv2179c has close structural homology to Escherichia coli RNase T. Consistent with the DEDD fold, Rv2179c has exoribonuclease activity, cleaving the 3' single-strand overhangs of duplex RNA. Functional orthologs of Rv2179c are prevalent in actinobacteria and found in bacteria as phylogenetically distant as proteobacteria. Thus, Rv2179c is the founding member of a new, large RNase family with hundreds of members across the bacterial kingdom.
PubMed: 24311791
DOI: 10.1074/jbc.M113.525683
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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