1LEP

THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROTEIN CHAPERONIN-10 OF MYCOBACTERIUM LEPRAE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.380 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.230 

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This is version 1.3 of the entry. See complete history. 


Literature

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.

Mande, S.C., Mehra, V., Bloom, B.R., Hol, W.G.

(1996) Science 271: 203-207

  • DOI: https://doi.org/10.1126/science.271.5246.203
  • Primary Citation of Related Structures:  
    1LEP

  • PubMed Abstract: 

    Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10 and in Escherichia coli GroES, play an important role in ensuring the proper folding of many proteins. The crystal structure of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a resolution of 3.5 angstroms. The architecture of the Ml-cpn10 heptamer resembles a dome with an oculus in its roof. The inner surface of the dome is hydrophilic and highly charged. A flexible region, known to interact with cpn60, extends from the lower rim of the dome. With the structure of a cpn10 heptamer now revealed and the structure of the E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed.

    • Organizational Affiliation: 

    Department of Biological Structure, University of Washington, Seattle 98195, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHAPERONIN-10
A, B, C, D, E
A, B, C, D, E, F, G
99Mycobacterium lepraeMutation(s): 0 
UniProt
Find proteins for P24301 (Mycobacterium leprae (strain TN))
Explore P24301 
Go to UniProtKB:  P24301
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24301
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.380 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.230 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.9α = 90
b = 129β = 90
c = 109.5γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-01-11
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Other