Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
Article Abstract:
The structure of the GTPase-containing segment of the functional homologue of the signal recognition particle (SRP) receptor of Escherichia coli, the Ftsy, at 2.2 angstrom resolution without bound nucleotide is described. This NG domain exhibits similarities to the Ras-related GTPases. It also shows features unique to the SRP-type GTPases, including a wide-open GTP-binding region, an independent amino-terminal domain and an insertion within the p21(super ras) effector domain. The low affinity of FtsY for GTp is explained by the structure.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
Article Abstract:
The promotion of GTP binding to the 54K subunit of signal-recognition particle (SRP) involves a ribosomal component. The SRP helps in the targeting of proteins to the endoplasmic reticulum. High-affinity interaction between SRP and its receptor in the ER membrane is possible in the presence of GTP-bound SRP54. The release of signal sequence from SRP, the placing of the nascent polypeptide chain into the translocation channel and GTP hydrolysis follow the interaction.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex
Article Abstract:
The ribonucleoprotein complex made up of the P48 protein and the 4.5S RNA of Escherichia coli interacts with a nascent secretory protein's signal sequence, which means it is a signal recognition particle. This ribonucleoprotein complex of Escherichia coli is strongly similar in its sequence to the 54K signal-sequence-binding protein and 7S RNA of mammalian signal recognition particle.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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