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PDBsum entry 2og2

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protein ligands metals links
Protein transport PDB id
2og2
Jmol
Contents
Protein chain
302 a.a. *
Ligands
MLI
Metals
_MG
Waters ×214
* Residue conservation analysis
PDB id:
2og2
Name: Protein transport
Title: Crystal structure of chloroplast ftsy from arabidopsis thaliana
Structure: Putative signal recognition particle receptor. Chain: a. Synonym: putative signal recognition particle receptor alpha subunit, chloroplast ftsy homolog. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Strain: wassilewskija ecotype. Gene: ftsy. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.213     R-free:   0.248
Authors: J.Chartron,S.Chandrasekar,P.J.Ampornpan,S.Shan
Key ref:
S.Chandrasekar et al. (2008). Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction. J Mol Biol, 375, 425-436. PubMed id: 18035371 DOI: 10.1016/j.jmb.2007.09.061
Date:
04-Jan-07     Release date:   11-Dec-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O80842  (CFTSY_ARATH) -  Cell division protein FtsY homolog, chloroplastic
Seq:
Struc:
366 a.a.
302 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     SRP-dependent cotranslational protein targeting to membrane   2 terms 
  Biochemical function     nucleotide binding     3 terms  

 

 
DOI no: 10.1016/j.jmb.2007.09.061 J Mol Biol 375:425-436 (2008)
PubMed id: 18035371  
 
 
Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction.
S.Chandrasekar, J.Chartron, P.Jaru-Ampornpan, S.O.Shan.
 
  ABSTRACT  
 
The signal recognition particle (SRP) pathway mediates co-translational targeting of nascent proteins to membranes. Chloroplast SRP is unique in that it does not contain the otherwise universally conserved SRP RNA, which accelerates the association between the SRP guanosine-5'-triphosphate (GTP) binding protein and its receptor FtsY in classical SRP pathways. Recently, we showed that the SRP and SRP receptor (SR) GTPases from chloroplast (cpSRP54 and cpFtsY, respectively) can interact with one another 400-fold more efficiently than their bacterial homologues, thus providing an explanation as to why this novel chloroplast SRP pathway bypasses the requirement for the SRP RNA. Here we report the crystal structure of cpFtsY from Arabidopsis thaliana at 2.0 A resolution. In this chloroplast SR, the N-terminal "N" domain is more tightly packed, and a more extensive interaction surface is formed between the GTPase "G" domain and the N domain than was previously observed in many of its bacterial homologues. As a result, the overall conformation of apo-cpFtsY is closer to that found in the bacterial SRP*FtsY complex than in free bacterial FtsY, especially with regard to the relative orientation of the N and G domains. In contrast, active-site residues in the G domain are mispositioned, explaining the low basal GTP binding and hydrolysis activity of free cpFtsY. This structure emphasizes proper N-G domain arrangement as a key factor in modulating the efficiency of SRP-receptor interaction and helps account, in part, for the faster kinetics at which the chloroplast SR interacts with its binding partner in the absence of an SRP RNA.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. G-domain superpositions of the structure of free (a) Taq FtsY (orange; 2Q9A) or (b) cpFtsY (green) onto that of the Taq Ffh·FtsY complex. The Ffh molecule in the complex is shown in brown, and the FtsY molecule in the complex is shown in tan. The superposition is done as in Fig. 2 and is described in Materials and Methods.
Figure 5.
Fig. 5. (a) Mutant cpFtsY F33L, F71V (•) is less active in interacting with cpSRP54 than wild-type cpFtsY (○). The reaction rate constants were determined and analyzed as described in the Methods using 100 nM SRP54 and 100 μM GTP.^41 (b) Mutant E. coli FtsY L199F, V240F (▪) is more active in interacting with Ffh than wild-type E. coli FtsY (□).
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2008, 375, 425-436) copyright 2008.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20018841 S.Falk, S.Ravaud, J.Koch, and I.Sinning (2010).
The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane.
  J Biol Chem, 285, 5954-5962.  
19187234 C.Aldridge, P.Cain, and C.Robinson (2009).
Protein transport in organelles: Protein transport into and across the thylakoid membrane.
  FEBS J, 276, 1177-1186.  
19293157 N.J.Marty, D.Rajalingam, A.D.Kight, N.E.Lewis, D.Fologea, T.K.Kumar, R.L.Henry, and R.L.Goforth (2009).
The Membrane-binding Motif of the Chloroplast Signal Recognition Particle Receptor (cpFtsY) Regulates GTPase Activity.
  J Biol Chem, 284, 14891-14903.  
19587121 P.Jaru-Ampornpan, T.X.Nguyen, and S.O.Shan (2009).
A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway.
  Mol Biol Cell, 20, 3965-3973.  
18978942 P.F.Egea, H.Tsuruta, G.P.de 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.  
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.