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Literature summary for 7.4.2.5 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)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
E485R/E488R/R367E mutation leads to a closed conformation of the clamp, the C-loop remains inside the clamp Thermotoga maritima
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

Organism UniProt Comment Textmining
Thermotoga maritima Q9X1R4
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Thermotoga maritima DSM 3109 Q9X1R4
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