1okk
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Two structurally homologous guanosine triphosphatase (GTPase) domains | + | Two structurally homologous guanosine triphosphatase (GTPase) domains interact directly during signal recognition particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The 2.05 angstrom structure of a complex of the NG GTPase domains of Ffh and FtsY reveals a remarkably symmetric heterodimer sequestering a composite active site that contains two bound nucleotides. The structure explains the coordinate activation of the two GTPases. Conformational changes coupled to formation of their extensive interface may function allosterically to signal formation of the targeting complex to the signal-sequence binding site and the translocon. We propose that the complex represents a molecular "latch" and that its disengagement is regulated by completion of assembly of the GTPase active site. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
| - | [[Category: Focia, P | + | [[Category: Focia, P J.]] |
| - | [[Category: Freymann, D | + | [[Category: Freymann, D M.]] |
[[Category: BZP]] | [[Category: BZP]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
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[[Category: srp]] | [[Category: srp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:50 2008'' |
Revision as of 12:18, 21 February 2008
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HOMO-HETERODIMERIC COMPLEX OF THE SRP GTPASES
Overview
Two structurally homologous guanosine triphosphatase (GTPase) domains interact directly during signal recognition particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The 2.05 angstrom structure of a complex of the NG GTPase domains of Ffh and FtsY reveals a remarkably symmetric heterodimer sequestering a composite active site that contains two bound nucleotides. The structure explains the coordinate activation of the two GTPases. Conformational changes coupled to formation of their extensive interface may function allosterically to signal formation of the targeting complex to the signal-sequence binding site and the translocon. We propose that the complex represents a molecular "latch" and that its disengagement is regulated by completion of assembly of the GTPase active site.
About this Structure
1OKK is a Protein complex structure of sequences from Thermus aquaticus with , , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Heterodimeric GTPase core of the SRP targeting complex., Focia PJ, Shepotinovskaya IV, Seidler JA, Freymann DM, Science. 2004 Jan 16;303(5656):373-7. PMID:14726591
Page seeded by OCA on Thu Feb 21 14:18:50 2008
Categories: Protein complex | Thermus aquaticus | Focia, P J. | Freymann, D M. | BZP | EDO | GCP | MG | SO4 | Ffh | Ftsy | Gtpase | Membrane targeting | Signal sequence recognition | Srp
