spacer
spacer

PDBsum entry 3gud

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Chaperone PDB id
3gud
Jmol
Contents
Protein chains
119 a.a. *
Ligands
PEG
Metals
_NA
_BR
_CL
Waters ×85
* Residue conservation analysis
PDB id:
3gud
Name: Chaperone
Title: Crystal structure of a novel intramolecular chaperon
Structure: Neck appendage protein. Chain: a, b. Engineered: yes
Source: Bacillus phage ga-1. Bacteriophage ga-1. Organism_taxid: 12345. Gene: gene 12. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.199     R-free:   0.232
Authors: E.C.Schulz,A.Dickmanns,R.Ficner
Key ref: E.C.Schulz et al. (2010). Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nat Struct Mol Biol, 17, 210-215. PubMed id: 20118935
Date:
29-Mar-09     Release date:   02-Feb-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9FZW3  (Q9FZW3_BPGA1) -  Neck appendage protein
Seq:
Struc:
 
Seq:
Struc:
740 a.a.
119 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Nat Struct Mol Biol 17:210-215 (2010)
PubMed id: 20118935  
 
 
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.
E.C.Schulz, A.Dickmanns, H.Urlaub, A.Schmitt, M.Mühlenhoff, K.Stummeyer, D.Schwarzer, R.Gerardy-Schahn, R.Ficner.
 
  ABSTRACT  
 
Protein folding is often mediated by molecular chaperones. Recently, a novel class of intramolecular chaperones has been identified in tailspike proteins of evolutionarily distant viruses, which require a C-terminal chaperone for correct folding. The highly homologous chaperone domains are interchangeable between pre-proteins and release themselves after protein folding. Here we report the crystal structures of two intramolecular chaperone domains in either the released or the pre-cleaved form, revealing the role of the chaperone domain in the formation of a triple-beta-helix fold. Tentacle-like protrusions enclose the polypeptide chains of the pre-protein during the folding process. After the assembly, a sensory mechanism for correctly folded beta-helices triggers a serine-lysine catalytic dyad to autoproteolytically release the mature protein. Sequence analysis shows a conservation of the intramolecular chaperones in functionally unrelated proteins sharing beta-helices as a common structural motif.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21330133 E.C.Schulz, and R.Ficner (2011).
Knitting and snipping: chaperones in β-helix folding.
  Curr Opin Struct Biol, 21, 232-239.  
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.