2M3G
Structure of Anabaena Sensory Rhodopsin Determined by Solid State NMR Spectroscopy
Summary for 2M3G
| Entry DOI | 10.2210/pdb2m3g/pdb |
| Descriptor | Anabaena Sensory Rhodopsin, RETINAL (2 entities in total) |
| Functional Keywords | solid state nmr, anabaena sensory rhodopsin, mas nmr, trimers, membrane protein |
| Biological source | Nostoc sp. PCC 7120 (Cyanobacteria) |
| Total number of polymer chains | 3 |
| Total formula weight | 82587.81 |
| Authors | Wang, S.,Munro, R.A.,Shi, L.,Kawamura, I.,Okitsu, T.,Wada, A.,Kim, S.,Jung, K.,Brown, L.S.,Ladizhansky, V. (deposition date: 2013-01-17, release date: 2013-08-21, Last modification date: 2024-10-16) |
| Primary citation | Wang, S.,Munro, R.A.,Shi, L.,Kawamura, I.,Okitsu, T.,Wada, A.,Kim, S.Y.,Jung, K.H.,Brown, L.S.,Ladizhansky, V. Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein. Nat.Methods, 10:1007-1012, 2013 Cited by PubMed Abstract: Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning solid-state NMR spectroscopy can be used to determine structures of membrane proteins reconstituted in synthetic lipids, an environment similar to the natural membrane. We combined a large number of experimentally determined interatomic distances and local torsional restraints to solve the structure of an oligomeric membrane protein of common seven-helical fold, Anabaena sensory rhodopsin (ASR). We determined the atomic resolution detail of the oligomerization interface of the ASR trimer, and the arrangement of helices, side chains and the retinal cofactor in the monomer. PubMed: 24013819DOI: 10.1038/nmeth.2635 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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