1ZU5
Crystal structure of FtsY from Mycoplasma mycoides- space group H32
1ZU5 の概要
| エントリーDOI | 10.2210/pdb1zu5/pdb |
| 関連するPDBエントリー | 1ZU4 |
| 分子名称 | ftsY (2 entities in total) |
| 機能のキーワード | gtpase, ftsy, signal recognition particle, srp, receptor, protein transport |
| 由来する生物種 | Mycoplasma mycoides |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 72269.17 |
| 構造登録者 | Gariani, T.,Samuelsson, T.,Sauer-Eriksson, A.E. (登録日: 2005-05-30, 公開日: 2006-01-24, 最終更新日: 2023-10-25) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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