1ZU5
Crystal structure of FtsY from Mycoplasma mycoides- space group H32
Summary for 1ZU5
| Entry DOI | 10.2210/pdb1zu5/pdb |
| Related | 1ZU4 |
| Descriptor | ftsY (2 entities in total) |
| Functional Keywords | gtpase, ftsy, signal recognition particle, srp, receptor, protein transport |
| Biological source | Mycoplasma mycoides |
| Total number of polymer chains | 2 |
| Total formula weight | 72269.17 |
| Authors | Gariani, T.,Samuelsson, T.,Sauer-Eriksson, A.E. (deposition date: 2005-05-30, release date: 2006-01-24, Last modification date: 2023-10-25) |
| Primary citation | Gariani, T.,Samuelsson, T.,Sauer-Eriksson, A.E. Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY J.Struct.Biol., 153:85-96, 2006 Cited by PubMed Abstract: The prokaryotic signal recognition particle Ffh and its receptor FtsY allow targeting of proteins into or across the plasma membrane. The targeting process is GTP dependent and the two proteins constitute a distinct GTPase family. The receptor FtsY is composed of A and NG domains where the NG's GTPase domain plays a critical role in the targeting process. In this study, we describe two X-ray structures determined independently of each other of the NG domain of FtsY from Mycoplasma mycoides (MmFtsY). The two structures are markedly different in three of the nucleotide-binding segments, GI (P-loop), GII, and GIII, making only one of the structures compatible with nucleotide binding. Interestingly, the two distinct conformations of the nucleotide-binding segments of MmFtsY are similar to the apo- and ADP-loaded forms of certain ATPases. The structure of the extended interface between the A and NG domains of MmFtsY provides new insights into the role of the A domain for phospholipid interaction. PubMed: 16343944DOI: 10.1016/j.jsb.2005.10.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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