Solution structure of GroEL and its complex with Rhodanese from small angle neutron scattering
Small angle neutron scattering measurements were made on Echerichia coli GroEL chaperonin and its complex with rhodanese in D{sub 2}O. GroEL contains 14 equivalent subunits arranged as two stacked seven-member rings. The radius of gyration from the experimental data agrees well with that obtained from the calculated form factor by using the coordinates of the x-ray structure of E coli GroEL. The x-ray crystal structure does not include about 5% of terminal amino acid residues so an equivalent protein volume was added inside the GroEL cavity and its location was determined. In addition, the best fit of the solution scattering data requires five degrees of flaring of the apical domains and the inclusion of small contributions from seven-subunit rings and monomers. The modeling of the SANS data for the GroEL/rhodanese complex supported a {open_quotes}champagne cork{close_quotes} model suggesting that rhodanese is bound across one opening of GroEL rather than inside its cavity.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE Office of Energy Research, Washington, DC (United States)
- DOE Contract Number:
- AC05-96OR22464; W-31109-ENG-38
- OSTI ID:
- 522758
- Report Number(s):
- ANL/CMB/PP-86547; ON: DE97008525; TRN: 97:005005
- Resource Relation:
- Other Information: PBD: [1997]
- Country of Publication:
- United States
- Language:
- English
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