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Literature summary for 3.6.5.4 extracted from

  • Shan, S.O.; Walter, P.
    Co-translational protein targeting by the signal recognition particle (2005), FEBS Lett., 579, 921-926.
    View publication on PubMed
Search for more literature for 3.6.5.4

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface Thermus aquaticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Thermus aquaticus the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate GDP + phosphate
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Organism

Organism UniProt Comment Textmining
Thermus aquaticus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
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 Thermus aquaticus GDP + phosphate
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GTP + H2O the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate Thermus aquaticus GDP + phosphate
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 ?