PDBsum entry 1zu5

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protein Protein-protein interface(s) links
Protein transport PDB id
Jmol PyMol
Protein chains
309 a.a. *
Waters ×139
* Residue conservation analysis
PDB id:
Name: Protein transport
Title: Crystal structure of ftsy from mycoplasma mycoides- space group h32
Structure: Ftsy. Chain: a, b. Fragment: ng domain. Synonym: srp receptor ftsy. Engineered: yes
Source: Mycoplasma mycoides. Organism_taxid: 2102. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Hexamer (from PQS)
2.40Å     R-factor:   0.212     R-free:   0.246
Authors: T.Gariani,T.Samuelsson,A.E.Sauer-Eriksson
Key ref: T.Gariani et al. (2006). Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY. J Struct Biol, 153, 85-96. PubMed id: 16343944 DOI: 10.1016/j.jsb.2005.10.003
30-May-05     Release date:   24-Jan-06    
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Protein chains
Pfam   ArchSchema ?
Q6MTB9  (FTSY_MYCMS) -  Signal recognition particle receptor FtsY
400 a.a.
309 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     SRP-dependent cotranslational protein targeting to membrane   1 term 
  Biochemical function     GTP binding     1 term  


DOI no: 10.1016/j.jsb.2005.10.003 J Struct Biol 153:85-96 (2006)
PubMed id: 16343944  
Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY.
T.Gariani, T.Samuelsson, A.E.Sauer-Eriksson.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19536595 H.J.Dong, J.Y.Jiang, and Y.Q.Li (2009).
The distinct anchoring mechanism of FtsY from different microbes.
  Curr Microbiol, 59, 336-340.  
18978942 P.F.Egea, H.Tsuruta, Leon, J.Napetschnig, P.Walter, and R.M.Stroud (2008).
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.
  PLoS ONE, 3, e3619.
PDB codes: 3dm9 3dmd 3e70
19172744 S.B.Neher, N.Bradshaw, S.N.Floor, J.D.Gross, and P.Walter (2008).
SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.
  Nat Struct Mol Biol, 15, 916-923.  
18931411 U.D.Ramirez, P.J.Focia, and D.M.Freymann (2008).
Nucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase Ffh.
  Acta Crystallogr D Biol Crystallogr, 64, 1043-1053.
PDB codes: 2c03 2c04
17926093 X.L.Shen, H.J.Dong, X.P.Hou, W.J.Guan, and Y.Q.Li (2008).
FtsY affects sporulation and antibiotic production by whiH in Streptomyces coelicolor.
  Curr Microbiol, 56, 61-65.  
17622352 C.L.Reyes, E.Rutenber, P.Walter, and R.M.Stroud (2007).
X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.
  PLoS ONE, 2, e607.
PDB codes: 2q9a 2q9b 2q9c
17699634 G.Bange, G.Petzold, K.Wild, R.O.Parlitz, and I.Sinning (2007).
The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP.
  Proc Natl Acad Sci U S A, 104, 13621-13625.
PDB codes: 2px0 2px3
17186523 J.Gawronski-Salerno, J.S.Coon, P.J.Focia, and D.M.Freymann (2007).
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.
PDB code: 2iyl
17726013 L.Bahari, R.Parlitz, A.Eitan, G.Stjepanovic, E.S.Bochkareva, I.Sinning, and E.Bibi (2007).
Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY.
  J Biol Chem, 282, 32168-32175.  
17726012 R.Parlitz, A.Eitan, G.Stjepanovic, L.Bahari, G.Bange, E.Bibi, and I.Sinning (2007).
Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.
  J Biol Chem, 282, 32176-32184.  
17139088 U.D.Ramirez, and D.M.Freymann (2006).
Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh.
  Acta Crystallogr D Biol Crystallogr, 62, 1520-1534.
PDB codes: 2j45 2j46
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.