Kaushal, Prem Singh and Singh, Pawan and Sharma, Alok and Muniyappa, K. and Vijayan, M. (2010) X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures. In: Acta Crystallographica Section D, 66 (Part 1). pp. 1048-1058.
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The crystal structures of two forms of Mycobacterium leprae single-stranded DNA-binding protein (SSB) have been determined at 2.05 and 2.8 A resolution. Comparison of these structures with the structures of other eubacterial SSBs indicates considerable variation in their quaternary association, although the DNA-binding domains in all of them exhibit the same OB-fold. This variation has no linear correlation with sequence variation, but could be related to variation in protein stability. Molecular-dynamics simulations have been carried out on tetrameric molecules derived from the two forms and the prototype Escherichia coli SSB and the individual subunits of both proteins. Together, the X-ray studies and molecular-dynamics simulations yield information on the relatively rigid and flexible regions of the molecule and on the effect of oligomerization on flexibility. The simulations provide insight into the changes in subunit structure on oligomerization. They also provide insight into the stability and time evolution of the hydrogen bonds/water bridges that connect the two pairs of monomers in the tetramer.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to International Union of Crystallography.|
|Keywords:||single-stranded DNA-binding proteins; Mycobacterium leprae; molecular dynamics|
|Department/Centre:||Division of Biological Sciences > Biochemistry
Division of Biological Sciences > Molecular Biophysics Unit
|Date Deposited:||08 Nov 2010 08:44|
|Last Modified:||08 Nov 2010 08:44|
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