1f6v
From Proteopedia
(New page: 200px<br /><applet load="1f6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f6v" /> '''SOLUTION STRUCTURE OF THE C TERMINAL OF MU B...) |
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| - | [[Image:1f6v.jpg|left|200px]]<br /><applet load="1f6v" size=" | + | [[Image:1f6v.jpg|left|200px]]<br /><applet load="1f6v" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN'''<br /> | '''SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mu B is one of four proteins required for the strand transfer step of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1F6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http:// | + | 1F6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chaconas, G.]] | [[Category: Chaconas, G.]] | ||
[[Category: Hung, L-H]] | [[Category: Hung, L-H]] | ||
| - | [[Category: Shaw, G | + | [[Category: Shaw, G S.]] |
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
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[[Category: transposition]] | [[Category: transposition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:31 2008'' |
Revision as of 10:35, 21 February 2008
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SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN
Overview
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.
About this Structure
1F6V is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
Reference
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
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