2REU

Crystal Structure of the C-terminal of Sau3AI fragment

Summary for 2REU

• Entry DOI: 10.2210/pdb2reu/pdb
• Descriptor: Type II restriction enzyme Sau3AI, MAGNESIUM ION (3 entities in total)
• Functional Keywords: helix, beta, random coil, endonuclease, hydrolase, magnesium, nuclease, restriction system
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 30417.60

Authors

Hu, X.,Yu, F.,Xu, C.,He, J. (deposition date: 2007-09-27, release date: 2008-09-30, Last modification date: 2024-03-13)

Primary citation

Xu, C.Y.,Yu, F.,Xu, S.J.,Ding, Y.,Sun, L.H.,Tang, L.,Hu, X.J.,Zhang, Z.H.,He, J.H.
Crystal structure and function of C-terminal Sau3AI domain
Biochim.Biophys.Acta, 1794:118-123, 2009

PubMed Abstract: Sau3AI is a type II restriction enzyme that recognizes the 5'-GATC-3' sequence in double-strand DNA and cleaves at 5' to the G residue. The C-terminal domain of Sau3AI (Sau3AI-C), which contains amino acids from 233 to 489, was crystallized and its structure was solved by using the Multi-wavelength Anomalous Diffraction method. The Sau3AI-C structure at 1.9 A resolution is similar to the structure of MutH, a DNA mismatch repair protein that shares high sequence similarity with the N-terminal Sau3AI domain. The functional analysis shows that Sau3AI-C can bind DNA with one recognition sequence but has no cleavage activity. These results indicate that Sau3AI is a pseudo-dimer belonging to the type IIe restriction enzymes and the Sau3AI-C is the allosteric effector domain that assists DNA binding and cleavage.

PubMed: 18930848
DOI: 10.1016/j.bbapap.2008.09.008

Experimental method

X-RAY DIFFRACTION (1.9 Å)