5K5D
Structure of the C2221 form of Pnob8-like ParB-N domain
Summary for 5K5D
| Entry DOI | 10.2210/pdb5k5d/pdb |
| Related | 5K5A |
| Descriptor | ParB domain protein nuclease, CITRIC ACID (3 entities in total) |
| Functional Keywords | parb-n, pnob8, partition, hydrolase |
| Biological source | Sulfolobus solfataricus |
| Total number of polymer chains | 3 |
| Total formula weight | 107294.54 |
| Authors | Schumacher, M. (deposition date: 2016-05-23, release date: 2016-06-15, Last modification date: 2023-11-15) |
| Primary citation | Schumacher, M.A.,Tonthat, N.K.,Lee, J.,Rodriguez-Castneda, F.A.,Chinnam, N.B.,Kalliomaa-Sanford, A.K.,Ng, I.W.,Barge, M.T.,Shaw, P.L.,Barilla, D. Structures of archaeal DNA segregation machinery reveal bacterial and eukaryotic linkages. Science, 349:1120-1124, 2015 Cited by PubMed Abstract: Although recent studies have provided a wealth of information about archaeal biology, nothing is known about the molecular basis of DNA segregation in these organisms. Here, we unveil the machinery and assembly mechanism of the archaeal Sulfolobus pNOB8 partition system. This system uses three proteins: ParA; an atypical ParB adaptor; and a centromere-binding component, AspA. AspA utilizes a spreading mechanism to create a DNA superhelix onto which ParB assembles. This supercomplex links to the ParA motor, which contains a bacteria-like Walker motif. The C domain of ParB harbors structural similarity to CenpA, which dictates eukaryotic segregation. Thus, this archaeal system combines bacteria-like and eukarya-like components, which suggests the possible conservation of DNA segregation principles across the three domains of life. PubMed: 26339031DOI: 10.1126/science.aaa9046 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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