2KLV
Membrane-bound structure of the Pf1 major coat protein in DHPC micelle
Summary for 2KLV
Entry DOI | 10.2210/pdb2klv/pdb |
Related | 1PJF |
Descriptor | Capsid protein G8P (1 entity in total) |
Functional Keywords | membrane protein, alignment, alpha helix, capsid protein, membrane, transmembrane, virion |
Biological source | Pseudomonas phage Pf1 (Bacteriophage Pf1) |
Cellular location | Virion (Potential): P03621 |
Total number of polymer chains | 1 |
Total formula weight | 4612.39 |
Authors | Park, S.,Son, W.,Mukhopadhyay, R.,Valafar, H.,Opella, S.J. (deposition date: 2009-07-08, release date: 2009-10-06, Last modification date: 2024-05-22) |
Primary citation | Park, S.H.,Son, W.S.,Mukhopadhyay, R.,Valafar, H.,Opella, S.J. Phage-induced alignment of membrane proteins enables the measurement and structural analysis of residual dipolar couplings with dipolar waves and lambda-maps. J.Am.Chem.Soc., 131:14140-14141, 2009 Cited by PubMed Abstract: At pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide gel alignment, Dipolar Waves can be used to directly assess the secondary structure and a lambda-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints. PubMed: 19761238DOI: 10.1021/ja905640d PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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