3S1S

Characterization and crystal structure of the type IIG restriction endonuclease BpuSI

Summary for 3S1S

• Entry DOI: 10.2210/pdb3s1s/pdb
• Descriptor: restriction endonuclease BpuSI, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: pd--(d/e)xk catalytic motif, gamma-n6m-adenosine methyltransferase, s-adenosyl-methionine binding, hydrolase, transferase
• Biological source: Bacillus pumilus
• Total number of polymer chains: 1
• Total formula weight: 106569.83

Authors

Shen, B.W.,Xu, D.,Chan, S.-H.,Zheng, Y.,Zhu, Y.,Xu, S.-Y.,Stoddard, B.L. (deposition date: 2011-05-16, release date: 2011-07-13, Last modification date: 2024-11-20)

Primary citation

Shen, B.W.,Xu, D.,Chan, S.H.,Zheng, Y.,Zhu, Z.,Xu, S.Y.,Stoddard, B.L.
Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSI.
Nucleic Acids Res., 39:8223-8236, 2011

PubMed Abstract: A type IIG restriction endonuclease, RM.BpuSI from Bacillus pumilus, has been characterized and its X-ray crystal structure determined at 2.35Å resolution. The enzyme is comprised of an array of 5-folded domains that couple the enzyme's N-terminal endonuclease domain to its C-terminal target recognition and methylation activities. The REase domain contains a PD-x(15)-ExK motif, is closely superimposable against the FokI endonuclease domain, and coordinates a single metal ion. A helical bundle domain connects the endonuclease and methyltransferase (MTase) domains. The MTase domain is similar to the N6-adenine MTase M.TaqI, while the target recognition domain (TRD or specificity domain) resembles a truncated S subunit of Type I R-M system. A final structural domain, that may form additional DNA contacts, interrupts the TRD. DNA binding and cleavage must involve large movements of the endonuclease and TRD domains, that are probably tightly coordinated and coupled to target site methylation status.

PubMed: 21724614
DOI: 10.1093/nar/gkr543

Experimental method

X-RAY DIFFRACTION (2.35 Å)