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PDBsum entry 1srv
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Chaperone PDB id
1srv

 

 

 

 

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Contents
Protein chain
145 a.a. *
Waters ×80
* Residue conservation analysis
PDB id:
1srv
Name: Chaperone
Title: Thermus thermophilus groel (hsp60 class) fragment (apical domain) comprising residues 192-336
Structure: Protein (groel (hsp60 class)). Chain: a. Fragment: apical domain, residues 191 - 376. Synonym: 60 kd chaperonin, protein cpn60. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 274. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.193     R-free:   0.257
Authors: M.A.Walsh,I.Dementieva,G.Evans,R.Sanishvili,A.Joachimiak
Key ref:
M.A.Walsh et al. (1999). Taking MAD to the extreme: ultrafast protein structure determination. Acta Crystallogr D Biol Crystallogr, 55, 1168-1173. PubMed id: 10329779 DOI: 10.1107/S0907444999003698
Date:
02-Mar-99     Release date:   12-Mar-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61491  (CH60_THETH) -  Chaperonin GroEL (Fragment) from Thermus thermophilus
Seq:
Struc: 		145 a.a.
145 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.6.1.7  - chaperonin ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
ATP
 + H2O
 + folded polypeptide
 = ADP
 + phosphate
 + unfolded polypeptide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1107/S0907444999003698 Acta Crystallogr D Biol Crystallogr 55:1168-1173 (1999)
PubMed id: 10329779  
 
 
Taking MAD to the extreme: ultrafast protein structure determination.
M.A.Walsh, I.Dementieva, G.Evans, R.Sanishvili, A.Joachimiak.
 
  ABSTRACT  
 
Multiwavelength anomalous diffraction data were measured in 23 min from a 16 kDa selenomethionyl substituted protein, producing experimental phases to 2.25 A resolution. The data were collected on a mosaic 3 x 3 charge-coupled device using undulator radiation from the Structural Biology Center 19ID beamline at the Argonne National Laboratory's Advanced Photon Source. The phases were independently obtained semiautomatically by two crystallographic program suites, CCP4 and CNS. The quality and speed of this data acquisition exemplify the opportunities at third-generation synchrotron sources for high-throughput protein crystal structure determination.
 
  Selected figure(s)  
 
Figure 3.
Figure 3 Residue-based real-space map correlation coefficient (RSCC; Brändén & Jones, 1990[Brändén, C.-I. & Jones, T. A. (1990). Nature (London), 343, 687-689.]) for the experimental and DM solvent-flattened electron-density maps for the AD of T. thermophilus chaperonin at 2.25 Å resolution.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1168-1173) copyright 1999.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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16498617 Y.Kim, N.Maltseva, I.Dementieva, F.Collart, D.Holzle, and A.Joachimiak (2006).
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11551462 U.Heinemann, G.Illing, and H.Oschkinat (2001).
High-throughput three-dimensional protein structure determination.
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10639129 M.Weik, R.B.Ravelli, G.Kryger, S.McSweeney, M.L.Raves, M.Harel, P.Gros, I.Silman, J.Kroon, and J.L.Sussman (2000).
Specific chemical and structural damage to proteins produced by synchrotron radiation.
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11042455 P.D.Adams, and R.W.Grosse-Kunstleve (2000).
Recent developments in software for the automation of crystallographic macromolecular structure determination.
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10745008 R.B.Ravelli, and S.M.McSweeney (2000).
The 'fingerprint' that X-rays can leave on structures.
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11006535 S.E.Ealick (2000).
Advances in multiple wavelength anomalous diffraction crystallography.
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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.

 

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