2c1l

From Proteopedia

---

Revision as of 19:37, 29 October 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 2c1l, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [[1]], with EC number [3.1.21.4]. 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

Page seeded by OCA on Mon Oct 29 21:42:10 2007