3nh2

From Proteopedia

Crystal structure of RNase T in complex with a stem DNA with a 3' overhang

PDB ID 3nh2

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Structural highlights

3nh2 is a 8 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNT_ECOLI Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis, especially in strains lacking other exoribonucleases.[HAMAP-Rule:MF_00157]

Publication Abstract from PubMed

RNA maturation relies on various exonucleases to remove nucleotides successively from the 5' or 3' end of nucleic acids. However, little is known regarding the molecular basis for substrate and cleavage preference of exonucleases. Our biochemical and structural analyses on RNase T-DNA complexes show that the RNase T dimer has an ideal architecture for binding a duplex with a short 3' overhang to produce a digestion product of a duplex with a 2-nucleotide (nt) or 1-nt 3' overhang, depending on the composition of the last base pair in the duplex. A 'C-filter' in RNase T screens out the nucleic acids with 3'-terminal cytosines for hydrolysis by inducing a disruptive conformational change at the active site. Our results reveal the general principles and the working mechanism for the final trimming step made by RNase T in the maturation of stable RNA and pave the way for the understanding of other DEDD family exonucleases.

Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation.,Hsiao YY, Yang CC, Lin CL, Lin JL, Duh Y, Yuan HS Nat Chem Biol. 2011 Feb 13. PMID:21317904^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hsiao YY, Yang CC, Lin CL, Lin JL, Duh Y, Yuan HS. Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation. Nat Chem Biol. 2011 Feb 13. PMID:21317904 doi:10.1038/nchembio.524