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Literature DB >> 9927651

Trimeric domain-swapped barnase.

Abstract

The structure of a trimeric domain-swapped form of barnase (EC 3.1. 27.3) was determined by x-ray crystallography at a resolution of 2.2 A from crystals of space group R32. Residues 1-36 of one molecule associate with residues 41-110 from another molecule related through threefold symmetry. The resulting cyclic trimer contains three protein folds that are very similar to those in monomeric barnase. Both swapped domains contain a nucleation site for folding. The formation of a domain-swapped trimer is consistent with the description of the folding process of monomeric barnase as the formation and subsequent association of two foldons.

Mesh：

Substances：

Year: 1999 PMID： 9927651 PMCID： PMC15308 DOI： 10.1073/pnas.96.3.818

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

19 in total

1. The CCP4 suite: programs for protein crystallography.

Authors:
Journal: Acta Crystallogr D Biol Crystallogr Date: 1994-09-01

2. Improved methods for building protein models in electron density maps and the location of errors in these models.

Authors: T A Jones; J Y Zou; S W Cowan; M Kjeldgaard
Journal: Acta Crystallogr A Date: 1991-03-01 Impact factor: 2.290

3. Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity.

Authors: J Sancho; A R Fersht
Journal: J Mol Biol Date: 1992-04-05 Impact factor: 5.469

Review 4. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.

Authors: L Serrano; J T Kellis; P Cann; A Matouschek; A R Fersht
Journal: J Mol Biol Date: 1992-04-05 Impact factor: 5.469

Review 5. The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.

Authors: A Matouschek; L Serrano; A R Fersht
Journal: J Mol Biol Date: 1992-04-05 Impact factor: 5.469

6. Surface, subunit interfaces and interior of oligomeric proteins.

Authors: J Janin; S Miller; C Chothia
Journal: J Mol Biol Date: 1988-11-05 Impact factor: 5.469

7. A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.

Authors: V L Arcus; S Vuilleumier; S M Freund; M Bycroft; A R Fersht
Journal: J Mol Biol Date: 1995-11-24 Impact factor: 5.469

8. The A-state of barnase.

Authors: J M Sanz; C M Johnson; A R Fersht
Journal: Biochemistry Date: 1994-09-20 Impact factor: 3.162

9. Molecular structure of a new family of ribonucleases.

Authors: Y Mauguen; R W Hartley; E J Dodson; G G Dodson; G Bricogne; C Chothia; A Jack
Journal: Nature Date: 1982-05-13 Impact factor: 49.962

10. Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.

Authors: A M Buckle; A R Fersht
Journal: Biochemistry Date: 1994-02-22 Impact factor: 3.162

19 in total

1. Structures of the two 3D domain-swapped RNase A trimers.

Authors: Yanshun Liu; Giovanni Gotte; Massimo Libonati; David Eisenberg
Journal: Protein Sci Date: 2002-02 Impact factor: 6.725

2. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.

Authors: R A Staniforth; S Giannini; L D Higgins; M J Conroy; A M Hounslow; R Jerala; C J Craven; J P Waltho
Journal: EMBO J Date: 2001-09-03 Impact factor: 11.598

10. Insights into Protein Sequence and Structure-Derived Features Mediating 3D Domain Swapping Mechanism using Support Vector Machine Based Approach.

Authors: Khader Shameer; Ganesan Pugalenthi; Krishna Kumar Kandaswamy; Ponnuthurai N Suganthan; Govindaraju Archunan; Ramanathan Sowdhamini
Journal: Bioinform Biol Insights Date: 2010-06-17

Trimeric domain-swapped barnase.

1. The CCP4 suite: programs for protein crystallography.

2. Improved methods for building protein models in electron density maps and the location of errors in these models.

3. Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity.

Review 4. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.

Review 5. The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.

6. Surface, subunit interfaces and interior of oligomeric proteins.

7. A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.

8. The A-state of barnase.

9. Molecular structure of a new family of ribonucleases.

10. Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.

1. Structures of the two 3D domain-swapped RNase A trimers.

2. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.

Review 3. 3D domain swapping: as domains continue to swap.

4. Protein simulations: the absorption spectrum of barnase point mutants.

5. Interaction energy based protein structure networks.

Review 6. The Landscape of Intertwined Associations in Homooligomeric Proteins.

7. Two independently folding units of Plasmodium profilin suggest evolution via gene fusion.

8. Evidence for intermolecular domain exchange in the Fab domains of dimer and oligomers of an IgG1 monoclonal antibody.

9. Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates.

10. Insights into Protein Sequence and Structure-Derived Features Mediating 3D Domain Swapping Mechanism using Support Vector Machine Based Approach.