1RWD

Backbone NMR Structure of a Mutant P. Furiosus Rubredoxin Using Residual Dipolar Couplings

Replaces:  1M2Y

Summary for 1RWD

• Entry DOI: 10.2210/pdb1rwd/pdb
• Related: 1M2Y
• NMR Information: BMRB: 5926
• Descriptor: Rubredoxin (1 entity in total)
• Functional Keywords: residual dipolar couplings, structural genomics, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, electron transport
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 5863.47

Authors

Tian, F.,Valafar, H.,Prestegard, J.H.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2003-12-16, release date: 2003-12-23, Last modification date: 2024-05-22)

Primary citation

Tian, F.,Valafar, H.,Prestegard, J.H.
A Dipolar Coupling Based Strategy for Simultaneous Resonance Assignment and Structure Determination of Protein Backbones
J.Am.Chem.Soc., 123:11791-11796, 2001

PubMed Abstract: A new approach for simultaneous protein backbone resonance assignment and structure determination by NMR is introduced. This approach relies on recent advances in high-resolution NMR spectroscopy that allow observation of anisotropic interactions, such as dipolar couplings, from proteins partially aligned in field ordered media. Residual dipolar couplings are used for both geometric information and a filter in the assembly of residues in a sequential manner. Experimental data were collected in less than one week on a small redox protein, rubredoxin, that was 15N enriched but not enriched above 1% natural abundance in 13C. Given the acceleration possible with partial 13C enrichment, the protocol described should provide a very rapid route to protein structure determination. This is critical for the structural genomics initiative where protein expression and structural determination in a high-throughput manner will be needed.

PubMed: 11716736
DOI: 10.1021/ja011806h

Experimental method

SOLUTION NMR