2IYL
Structure of an FtsY:GDP complex
Summary for 2IYL
| Entry DOI | 10.2210/pdb2iyl/pdb |
| Related | 1FTS 1NG1 1OKK 1RJ9 1VMA 1ZU4 2CNW |
| Descriptor | CELL DIVISION PROTEIN FTSY, GUANOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | inner membrane, ribonucleoprotein, nucleotide-binding, signal recognition particle, srp, gdp, ffh, ftsy, gtpase, rna-binding, gtp-binding, cell division, membrane, cell cycle |
| Biological source | THERMUS AQUATICUS |
| Total number of polymer chains | 1 |
| Total formula weight | 31399.91 |
| Authors | Focia, P.J.,Freymann, D.M. (deposition date: 2006-07-18, release date: 2007-01-02, Last modification date: 2023-12-13) |
| Primary citation | Gawronski-Salerno, J.,Coon 5th., J.S.,Focia, P.J.,Freymann, D.M. X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases. Proteins, 66:984-995, 2007 Cited by PubMed Abstract: FtsY and Ffh are structurally similar prokaryotic Signal Recognition Particle GTPases that play an essential role in the Signal Recognition Particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The two GTPases assemble in a GTP-dependent manner to form a heterodimeric SRP targeting complex. We report here the 2.1 A X-ray structure of FtsY from T. aquaticus bound to GDP. The structure of the monomeric protein reveals, unexpectedly, canonical binding interactions for GDP. A comparison of the structures of the monomeric and complexed FtsY NG GTPase domain suggests that it undergoes a conformational change similar to that of Ffh NG during the assembly of the symmetric heterodimeric complex. However, in contrast to Ffh, in which the C-terminal helix shifts independently of the other subdomains, the C-terminal helix and N domain of T. aquaticus FtsY together behave as a rigid body during assembly, suggesting distinct mechanisms by which the interactions of the NG domain "module" are regulated in the context of the two SRP GTPases. PubMed: 17186523DOI: 10.1002/prot.21200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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