1F6V
SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN
Summary for 1F6V
| Entry DOI | 10.2210/pdb1f6v/pdb |
| Descriptor | DNA TRANSPOSITION PROTEIN (1 entity in total) |
| Functional Keywords | mu phage, recombination, transposition, atpase, dna binding, high salt, solution structure, dna binding protein |
| Biological source | Enterobacteria phage Mu |
| Cellular location | Host cytoplasm : P03763 |
| Total number of polymer chains | 1 |
| Total formula weight | 10237.76 |
| Authors | Hung, L.-H.,Chaconas, G.,Shaw, G.S. (deposition date: 2000-06-23, release date: 2000-11-08, Last modification date: 2024-05-01) |
| Primary citation | Hung, L.H.,Chaconas, G.,Shaw, G.S. The solution structure of the C-terminal domain of the Mu B transposition protein. EMBO J., 19:5625-5634, 2000 Cited by PubMed Abstract: 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. PubMed: 11060014DOI: 10.1093/emboj/19.21.5625 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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