4C7O
The structural basis of FtsY recruitment and GTPase activation by SRP RNA
Summary for 4C7O
| Entry DOI | 10.2210/pdb4c7o/pdb |
| Descriptor | SIGNAL RECOGNITION PARTICLE PROTEIN, SIGNAL RECOGNITION PARTICLE RECEPTOR FTSY, SRP RNA, ... (7 entities in total) |
| Functional Keywords | nuclear protein-rna complex, nuclear protein, protein translocation, signal recognition particle, signal recognition particle receptor, gdp alf3/4, nuclear protein/rna |
| Biological source | ESCHERICHIA COLI More |
| Cellular location | Cytoplasm: P0AGD7 Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10121 |
| Total number of polymer chains | 5 |
| Total formula weight | 143564.60 |
| Authors | Voigts-Hoffmann, F.,Schmitz, N.,Shen, K.,Shan, S.O.,Ataide, S.F.,Ban, N. (deposition date: 2013-09-23, release date: 2013-11-20, Last modification date: 2023-12-20) |
| Primary citation | Voigts-Hoffmann, F.,Schmitz, N.,Shen, K.,Shan, S.O.,Ataide, S.F.,Ban, N. The Structural Basis of Ftsy Recruitment and Gtpase Activation by Srp RNA Mol.Cell, 52:643-, 2013 Cited by PubMed Abstract: The universally conserved signal recognition particle (SRP) system mediates the targeting of membrane proteins to the translocon in a multistep process controlled by GTP hydrolysis. Here we present the 2.6 Å crystal structure of the GTPase domains of the E. coli SRP protein (Ffh) and its receptor (FtsY) in complex with the tetraloop and the distal region of SRP-RNA, trapped in the activated state in presence of GDP:AlF4. The structure reveals the atomic details of FtsY recruitment and, together with biochemical experiments, pinpoints G83 as the key RNA residue that stimulates GTP hydrolysis. Insertion of G83 into the FtsY active site orients a single glutamate residue provided by Ffh (E277), triggering GTP hydrolysis and complex disassembly at the end of the targeting cycle. The complete conservation of the key residues of the SRP-RNA and the SRP protein implies that the suggested chemical mechanism of GTPase activation is applicable across all kingdoms. PubMed: 24211265DOI: 10.1016/J.MOLCEL.2013.10.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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