1yt3
From Proteopedia
|
Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing
Overview
RNase D (RND) is one of seven exoribonucleases identified in Escherichia, coli. RNase D has homologs in many eubacteria and eukaryotes, and has been, shown to contribute to the 3' maturation of several stable RNAs. Here, we, report the 1.6 A resolution crystal structure of E. coli RNase D. The, conserved DEDD residues of RNase D fold into an arrangement very similar, to the Klenow fragment exonuclease domain. Besides the catalytic domain, RNase D also contains two structurally similar alpha-helical domains with, no discernible sequence homology between them. These closely resemble the, HRDC domain previously seen in RecQ-family helicases and several other, proteins acting on nucleic acids. More interestingly, the DEDD catalytic, domain and the two helical domains come together to form a ring-shaped, structure. The ring-shaped architecture of E. coli RNase D and the HRDC, domains likely play a major role in determining the substrate specificity, of this exoribonuclease.
About this Structure
1YT3 is a Single protein structure of sequence from Escherichia coli with SO4 and ZN as ligands. Active as Ribonuclease III, with EC number 3.1.26.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing., Zuo Y, Wang Y, Malhotra A, Structure. 2005 Jul;13(7):973-84. PMID:16004870
Page seeded by OCA on Wed Nov 21 07:02:15 2007
