2c1l

From Proteopedia

Revision as of 14:50, 30 October 2007

STRUCTURE OF THE BFII RESTRICTION ENDONUCLEASE

Overview

Among all restriction endonucleases known to date, BfiI is unique in, cleaving DNA in the absence of metal ions. BfiI represents a different, evolutionary lineage of restriction enzymes, as shown by its crystal, structure at 1.9-A resolution. The protein consists of two structural, domains. The N-terminal catalytic domain is similar to Nuc, an, EDTA-resistant nuclease from the phospholipase D superfamily. The, C-terminal DNA-binding domain of BfiI exhibits a beta-barrel-like, structure very similar to the effector DNA-binding domain of the, Mg(2+)-dependent restriction enzyme EcoRII and to the B3-like DNA-binding, domain of plant transcription factors. BfiI presumably evolved through, domain fusion of a DNA-recognition element to a nonspecific nuclease akin, to Nuc and elaborated a ... [(full description)]

About this Structure

2C1L is a [Single protein] structure of sequence from [Bacillus firmus] with TAR, BCT, TRS, TLA, SRT, MES and GOL as [ligands]. Active as [Type II site-specific deoxyribonuclease], with EC number [3.1.21.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease., Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V, Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15797-802. Epub 2005 Oct 24. PMID:16247004

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