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5G5T

Structure of the Argonaute protein from Methanocaldcoccus janaschii in complex with guide DNA

Summary for 5G5T
Entry DOI10.2210/pdb5g5t/pdb
Related5G5S
DescriptorARGONAUTE, GUIDE DNA, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordshydrolase-dna complex, argonaute, bacterial defense, hydrolase/dna
Biological sourceMETHANOCALDOCOCCUS JANNASCHII
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Total number of polymer chains2
Total formula weight91991.96
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: 2024-01-10)
Primary citationWillkomm, 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: 28319084
DOI: 10.1038/nmicrobiol.2017.35
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.85 Å)
Structure validation

226707

數據於2024-10-30公開中

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