3AFQ
Crystal structure of the single-stranded DNA binding protein from Mycobacterium leprae (Form II)
Summary for 3AFQ
| Entry DOI | 10.2210/pdb3afq/pdb |
| Related | 3AFP |
| Descriptor | Single-stranded DNA-binding protein (2 entities in total) |
| Functional Keywords | ob-fold, quaternary structure and stability, changes on oligomerisation, water-bridges, dna damage, dna repair, dna replication, dna-binding, dna binding protein |
| Biological source | Mycobacterium leprae |
| Total number of polymer chains | 4 |
| Total formula weight | 70878.00 |
| Authors | Kaushal, P.S.,Singh, P.,Sharma, A.,Muniyappa, K.,Vijayan, M. (deposition date: 2010-03-10, release date: 2010-10-06, Last modification date: 2023-11-01) |
| Primary citation | Kaushal, P.S.,Singh, P.,Sharma, A.,Muniyappa, K.,Vijayan, M. X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures Acta Crystallogr.,Sect.D, 66:1048-1058, 2010 Cited by PubMed Abstract: The crystal structures of two forms of Mycobacterium leprae single-stranded DNA-binding protein (SSB) have been determined at 2.05 and 2.8 Å 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. PubMed: 20944238DOI: 10.1107/S0907444910032208 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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