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2LEG

Membrane protein complex DsbB-DsbA structure by joint calculations with solid-state NMR and X-ray experimental data

Summary for 2LEG
Entry DOI10.2210/pdb2leg/pdb
Related2hi7
NMR InformationBMRB: 17710
DescriptorThiol:disulfide interchange protein DsbA, Disulfide bond formation protein B, ZINC ION, ... (4 entities in total)
Functional Keywordsdisulfide bond, membrane protein, redox-active center, cell inner membrane, cell membrane, chaperone, electron transport, membrane, oxidoreductase, transmembrane, transport
Biological sourceEscherichia coli
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Cellular locationPeriplasm: P0AEG4
Cell inner membrane; Multi-pass membrane protein: P0A6M2
Total number of polymer chains2
Total formula weight41545.64
Authors
Tang, M.,Sperling, L.J.,Berthold, D.A.,Schwieters, C.D.,Nesbitt, A.E.,Nieuwkoop, A.J.,Gennis, R.B.,Rienstra, C.M. (deposition date: 2011-06-15, release date: 2011-10-26, Last modification date: 2024-11-06)
Primary citationTang, M.,Sperling, L.J.,Berthold, D.A.,Schwieters, C.D.,Nesbitt, A.E.,Nieuwkoop, A.J.,Gennis, R.B.,Rienstra, C.M.
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.
J.Biomol.Nmr, 51:227-233, 2011
Cited by
PubMed Abstract: X-ray diffraction and nuclear magnetic resonance spectroscopy (NMR) are the staple methods for revealing atomic structures of proteins. Since crystals of biomolecular assemblies and membrane proteins often diffract weakly and such large systems encroach upon the molecular tumbling limit of solution NMR, new methods are essential to extend structures of such systems to high resolution. Here we present a method that incorporates solid-state NMR restraints alongside of X-ray reflections to the conventional model building and refinement steps of structure calculations. Using the 3.7 Å crystal structure of the integral membrane protein complex DsbB-DsbA as a test case yielded a significantly improved backbone precision of 0.92 Å in the transmembrane region, a 58% enhancement from using X-ray reflections alone. Furthermore, addition of solid-state NMR restraints greatly improved the overall quality of the structure by promoting 22% of DsbB transmembrane residues into the most favored regions of Ramachandran space in comparison to the crystal structure. This method is widely applicable to any protein system where X-ray data are available, and is particularly useful for the study of weakly diffracting crystals.
PubMed: 21938394
DOI: 10.1007/s10858-011-9565-6
PDB entries with the same primary citation
Experimental method
SOLID-STATE NMR
Structure validation

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