4EOG
Crystal structure of Csx1 of Pyrococcus furiosus
Summary for 4EOG
| Entry DOI | 10.2210/pdb4eog/pdb |
| Descriptor | Putative uncharacterized protein, ZINC ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | beta-hairpin, nucleic acid binding protein, rna binding, dna binding protein |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 1 |
| Total formula weight | 56962.08 |
| Authors | |
| Primary citation | Kim, Y.K.,Kim, Y.G.,Oh, B.H. Crystal structure and nucleic acid-binding activity of the CRISPR-associated protein Csx1 of Pyrococcus furiosus. Proteins, 81:261-270, 2013 Cited by PubMed Abstract: In many prokaryotic organisms, chromosomal loci known as clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (CAS) genes comprise an acquired immune defense system against invading phages and plasmids. Although many different Cas protein families have been identified, the exact biochemical functions of most of their constituents remain to be determined. In this study, we report the crystal structure of PF1127, a Cas protein of Pyrococcus furiosus DSM 3638 that is composed of 480 amino acids and belongs to the Csx1 family. The C-terminal domain of PF1127 has a unique β-hairpin structure that protrudes out of an α-helix and contains several positively charged residues. We demonstrate that PF1127 binds double-stranded DNA and RNA and that this activity requires an intact β-hairpin and involve the homodimerization of the protein. In contrast, another Csx1 protein from Sulfolobus solfataricus P2 that is composed of 377 amino acids does not have the β-hairpin structure and exhibits no DNA-binding properties under the same experimental conditions. Notably, the C-terminal domain of these two Csx1 proteins is greatly diversified, in contrast to the conserved N-terminal domain, which appears to play a common role in the homodimerization of the protein. Thus, although P. furiosus Csx1 is identified as a nucleic acid-binding protein, other Csx1 proteins are predicted to exhibit different individual biochemical activities. PubMed: 22987782DOI: 10.1002/prot.24183 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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