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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 ... [(full description)]
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
Page seeded by OCA on Tue Oct 30 17:03:59 2007
