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PDBsum entry 3ui2

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protein Protein-protein interface(s) links
Transport protein PDB id
3ui2

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
234 a.a.
13 a.a.
PDB id:
3ui2
Name: Transport protein
Title: Crystal structure of the cpsrp54 tail bound to cpsrp43
Structure: Signal recognition particle 43 kda protein, chloroplastic. Chain: a. Fragment: unp residues 84-327. Synonym: chromo protein srp43, cpsrp43. Engineered: yes. Signal recognition particle 54 kda protein, chloroplastic. Chain: b. Fragment: rrkr motif, unp residues 528-540. Synonym: 54 chloroplast protein, 54cp, srp54, cpsrp54, ffc.
Source: Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: at2g47450, cao, cpsrp43, t30b22.25. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: at5g03940, cpsrp54, f8f6_150, ffc.
Resolution:
3.18Å     R-factor:   0.210     R-free:   0.268
Authors: I.Holdermann,K.Wild,I.Sinning
Key ref: I.Holdermann et al. (2012). Chromodomains read the arginine code of post-translational targeting. Nat Struct Biol, 19, 260-263. PubMed id: 22231402
Date:
04-Nov-11     Release date:   11-Jan-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O22265  (SR43C_ARATH) -  Signal recognition particle 43 kDa protein, chloroplastic from Arabidopsis thaliana
Seq:
Struc:
373 a.a.
234 a.a.
Protein chain
Pfam   ArchSchema ?
P37107  (SR54C_ARATH) -  Signal recognition particle subunit SRP54, chloroplastic from Arabidopsis thaliana
Seq:
Struc:
 
Seq:
Struc:
564 a.a.
13 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain B: E.C.3.6.5.4  - signal-recognition-particle GTPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: GTP + H2O = GDP + phosphate + H+
GTP
+ H2O
= GDP
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Nat Struct Biol 19:260-263 (2012)
PubMed id: 22231402  
 
 
Chromodomains read the arginine code of post-translational targeting.
I.Holdermann, N.H.Meyer, A.Round, K.Wild, M.Sattler, I.Sinning.
 
  ABSTRACT  
 
No abstract given.

 

 

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