5G5S
Structure of the Argonaute protein from Methanocaldcoccus janaschii
Summary for 5G5S
| Entry DOI | 10.2210/pdb5g5s/pdb |
| Related | 5G5T |
| Descriptor | ARGONAUTE, MAGNESIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
| Functional Keywords | hydrolase, argonaute, bacterial defense |
| Biological source | METHANOCALDOCOCCUS JANNASCHII |
| Total number of polymer chains | 1 |
| Total formula weight | 85101.67 |
| Authors | Schneider, S.,Oellig, C.A.,Keegan, R.,Grohmann, D.,Zander, A.,Willkomm, S. (deposition date: 2016-06-03, release date: 2017-02-08, Last modification date: 2024-05-08) |
| Primary citation | Willkomm, S.,Oellig, C.A.,Zander, A.,Restle, T.,Keegan, R.,Grohmann, D.,Schneider, S. Structural and mechanistic insights into an archaeal DNA-guided Argonaute protein. Nat Microbiol, 2:17035-17035, 2017 Cited by PubMed Abstract: Argonaute (Ago) proteins in eukaryotes are known as key players in post-transcriptional gene silencing, while recent studies on prokaryotic Agos hint at their role in the protection against invading DNA. Here, we present crystal structures of the apo enzyme and a binary Ago-guide complex of the archaeal Methanocaldococcus jannaschii (Mj) Ago. Binding of a guide DNA leads to large structural rearrangements. This includes the structural transformation of a hinge region containing a switch helix, which has been shown for human Ago2 to be critical for the dynamic target search process. To identify key residues crucial for MjAgo function, we analysed the effect of several MjAgo mutants. We observe that the nature of the 3' and 5' nucleotides in particular, as well as the switch helix, appear to impact MjAgo cleavage activity. In summary, we provide insights into the molecular mechanisms that drive DNA-guided DNA silencing by an archaeal Ago. PubMed: 28319084DOI: 10.1038/nmicrobiol.2017.35 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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