2cbn
From Proteopedia
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CRYSTAL STRUCTURE OF ZIPD FROM ESCHERICHIA COLI
Overview
The elaC gene product from Escherichia coli, ZiPD, is a 3' tRNA-processing, endonuclease belonging to the tRNase Z family of enzymes that have been, identified in a wide variety of organisms. In contrast to the elaC, homologue from Bacillus subtilis, E. coli elaC is not essential for, viability, and although both enzymes process only precursor tRNA, (pre-tRNA) lacking a CCA triplet at the 3' end in vitro, the physiological, role of ZiPD remains enigmatic because all pre-tRNA species in E. coli are, transcribed with the CCA triplet. We present the first crystal structure, of ZiPD determined by multiple anomalous diffraction at a resolution of, 2.9 A. This structure shares many features with the tRNase Z enzymes from, B. subtilis and Thermotoga maritima, but there are distinct differences in, metal binding and overall domain organization. Unlike the previously, described homologous structures, ZiPD dimers display crystallographic, symmetry and fully loaded metal sites. The ZiPD exosite is similar to that, of the B. subtilis enzyme structurally, but its position with respect to, the protein core differs substantially, illustrating its ability to act as, a clamp in binding tRNA. Furthermore, the ZiPD crystal structure presented, here provides insight into the enzyme's cooperativity and assists the, ongoing attempt to elucidate the physiological function of this protein.
About this Structure
2CBN is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as Ribonuclease Z, with EC number 3.1.26.11 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins., Kostelecky B, Pohl E, Vogel A, Schilling O, Meyer-Klaucke W, J Bacteriol. 2006 Feb;188(4):1607-14. PMID:16452444
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