6HZ4
Structure of McrBC without DNA binding domains (one half of the full complex)
Summary for 6HZ4
| Entry DOI | 10.2210/pdb6hz4/pdb |
| EMDB information | 0310 |
| Descriptor | 5-methylcytosine-specific restriction enzyme B, Protein McrC, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | aaa+ superfamily, restriction enzyme, dna binding protein |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 8 |
| Total formula weight | 298807.31 |
| Authors | Itoh, Y.,Nirwan, N.,Saikrishnan, K.,Amunts, A. (deposition date: 2018-10-22, release date: 2019-07-24, Last modification date: 2024-05-15) |
| Primary citation | Nirwan, N.,Itoh, Y.,Singh, P.,Bandyopadhyay, S.,Vinothkumar, K.R.,Amunts, A.,Saikrishnan, K. Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC. Nat Commun, 10:3058-3058, 2019 Cited by PubMed Abstract: The AAA+ GTPase McrB powers DNA cleavage by the endonuclease McrC. The GTPase itself is activated by McrC. The architecture of the GTPase and nuclease complex, and the mechanism of their activation remained unknown. Here, we report a 3.6 Å structure of a GTPase-active and DNA-binding deficient construct of McrBC. Two hexameric rings of McrB are bridged by McrC dimer. McrC interacts asymmetrically with McrB protomers and inserts a stalk into the pore of the ring, reminiscent of the γ subunit complexed to αβ of F-ATPase. Activation of the GTPase involves conformational changes of residues essential for hydrolysis. Three consecutive nucleotide-binding pockets are occupied by the GTP analogue 5'-guanylyl imidodiphosphate and the next three by GDP, which is suggestive of sequential GTP hydrolysis. PubMed: 31296862DOI: 10.1038/s41467-019-11084-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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