Structural highlights
Function
[VPB_BPMU] This protein is a non-specific DNA-binding and ATP-hydrolyzing protein essential for bacteriophage integration and replication.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mu B is one of four proteins required for the strand transfer step of bacteriophage Mu DNA transposition and the only one where no high resolution structural data is available. Structural work on Mu B has been hampered primarily by solubility problems and its tendency to aggregate. We have overcome this problem by determination of the three-dimensional structure of the C-terminal domain of Mu B (B(223-312)) in 1.5 M NaCl using NMR spectroscopic methods. The structure of Mu B(223-312) comprises four helices (backbone r.m.s.d. 0.46 A) arranged in a loosely packed bundle and resembles that of the N-terminal region of the replication helicase, DnaB. This structural motif is likely to be involved in the inter-domainal regulation of ATPase activity for both Mu A and DnaB. The approach described here for structural determination in high salt may be generally applicable for proteins that do not crystallize and that are plagued by solubility problems at low ionic strength.
The solution structure of the C-terminal domain of the Mu B transposition protein.,Hung LH, Chaconas G, Shaw GS EMBO J. 2000 Nov 1;19(21):5625-34. PMID:11060014[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hung LH, Chaconas G, Shaw GS. The solution structure of the C-terminal domain of the Mu B transposition protein. EMBO J. 2000 Nov 1;19(21):5625-34. PMID:11060014 doi:10.1093/emboj/19.21.5625
