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PDBsum entry 1fts
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Signal recognition particle receptor
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PDB id
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1fts
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the ng domain from the signal-Recognition particle receptor ftsy.
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Authors
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G.Montoya,
C.Svensson,
J.Luirink,
I.Sinning.
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Ref.
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Nature, 1997,
385,
365-368.
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PubMed id
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Abstract
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Newly synthesized proteins destined either for secretion or incorporation into
membranes are targeted to the membrane translocation machinery by a ubiquitous
system consisting of a signal-recognition particle (SRP) and its receptor. Both
the SRP receptor and the protein within the SRP that binds the signal sequence
contain GTPases. These two proteins, together with the RNA component of the SRP,
form a complex and thereby regulate each other's GTPase activity. Here we report
the structure of the GTPase-containing portion of FtsY, the functional homologue
of the SRP receptor of Escherichia coli, at 2.2 A resolution without bound
nucleotide. This so-called NG domain displays similarities to the Ras-related
GTPases, as well as features unique to the SRP-type GTPases, such as a separate
amino-terminal domain, an insertion within the p21ras (Ras) effector domain, and
a wide-open GTP-binding region. The structure explains the low affinity of FtsY
for GTP, and suggests rearrangements that may occur on nucleotide binding. It
also identifies regions potentially involved in the transmission of signals
between domains and in interactions with regulatory proteins.
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Secondary reference #1
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Title
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Crystal structure of the ng domain from the signal-Recognition particle receptor ftsy.
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Authors
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G.Montoya,
C.Svensson,
J.Luirink,
I.Sinning.
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Ref.
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Nature, 1997,
385,
365-368.
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PubMed id
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