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PDBsum entry 1f6v

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protein links
DNA binding protein PDB id
1f6v
Jmol
Contents
Protein chain
91 a.a. *
* Residue conservation analysis
PDB id:
1f6v
Name: DNA binding protein
Title: Solution structure of thE C terminal of mu b transposition protein
Structure: DNA transposition protein. Chain: a. Fragment: c-terminal domain. Synonym: mu b transposition protein. Engineered: yes
Source: Enterobacteria phage mu. Organism_taxid: 10677. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: t7 phage
NMR struc: 20 models
Authors: L-H Hung,G.Chaconas,G.S.Shaw
Key ref:
L.H.Hung et al. (2000). The solution structure of the C-terminal domain of the Mu B transposition protein. EMBO J, 19, 5625-5634. PubMed id: 11060014 DOI: 10.1093/emboj/19.21.5625
Date:
23-Jun-00     Release date:   08-Nov-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03763  (VPB_BPMU) -  ATP-dependent target DNA activator B
Seq:
Struc:
312 a.a.
91 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.6.1.3  - Adenosinetriphosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate
ATP
+ H(2)O
= ADP
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     transposition, DNA-mediated   1 term 
  Biochemical function     DNA binding     1 term  

 

 
    reference    
 
 
DOI no: 10.1093/emboj/19.21.5625 EMBO J 19:5625-5634 (2000)
PubMed id: 11060014  
 
 
The solution structure of the C-terminal domain of the Mu B transposition protein.
L.H.Hung, G.Chaconas, G.S.Shaw.
 
  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.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 500 MHz ^1H-^15N HSQC spectrum of uniformly ^15N-labeled Mu B[223–312] in 20 mM Na[2]HPO[4], 1.5 M NaCl pH 6.8 at 25°C. Residue assignments are labelled according to sequence numbering for the intact protein. Side chain resonances are each connected with a line and labelled in parentheses. The box indicates the position of the E290 crosspeak that is visible at higher contour levels.
Figure 6.
Figure 6 Poisson–Boltzmann charge distribution for Mu B[223–312] calculated using GRASP (Nicholls, 1992). (A) The charge distribution was mapped to the Connolly surface of Mu B[223–312] with positively charged basic (blue) and negatively charged acidic (red) areas indicated. (B) Same as (A) but rotated 120° in a clockwise direction around the x-axis. On the right side of each surface diagram is a ribbon representation showing the side chains of basic residues found at the surface of the protein.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 5625-5634) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
12791691 C.J.Coros, Y.Sekino, T.A.Baker, and G.Chaconas (2003).
Effect of mutations in the C-terminal domain of Mu B on DNA binding and interactions with Mu A transposase.
  J Biol Chem, 278, 31210-31217.  
11889053 E.C.Greene, and K.Mizuuchi (2002).
Dynamics of a protein polymer: the assembly and disassembly pathways of the MuB transposition target complex.
  EMBO J, 21, 1477-1486.  
11298282 L.A.Roldan, and T.A.Baker (2001).
Differential role of the Mu B protein in phage Mu integration vs. replication: mechanistic insights into two transposition pathways.
  Mol Microbiol, 40, 141-155.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.