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Literature summary extracted from

  • Chen, Y.; Bauer, B.W.; Rapoport, T.A.; Gumbart, J.C.
    Conformational changes of the clamp of the protein translocation ATPase SecA (2015), J. Mol. Biol., 427, 2348-2359.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.4.2.5 to 1.9 A resolution. Structure represents an intermediate state during the transition of the clamp from an open to a closed conformation. Closure of the clamp occurs in two phases, an initial movement of polypeptide cross-linking domain PPXD, helical scaffold domain HSD, and helical wing domain HWD as a unit, followed by a movement of PPXD alone toward nucleotide-binding domain NBD2. The substrate associates with the back of the clamp by dynamic hydrogen bonding and the clamp is laterally closed by a conserved loop of the PPXD Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
7.4.2.5 E485R/E488R/R367E mutation leads to a closed conformation of the clamp, the C-loop remains inside the clamp Thermotoga maritima
7.4.2.5 R367E mutation of a conserved residue, results in significant lateral opening of the clamp, which leads to increased dissociation of the substrate Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
7.4.2.5 Thermotoga maritima Q9X1R4
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7.4.2.5 Thermotoga maritima DSM 3109 Q9X1R4
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