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2KLV

Membrane-bound structure of the Pf1 major coat protein in DHPC micelle

Summary for 2KLV
Entry DOI10.2210/pdb2klv/pdb
Related1PJF
DescriptorCapsid protein G8P (1 entity in total)
Functional Keywordsmembrane protein, alignment, alpha helix, capsid protein, membrane, transmembrane, virion
Biological sourcePseudomonas phage Pf1 (Bacteriophage Pf1)
Cellular locationVirion (Potential): P03621
Total number of polymer chains1
Total formula weight4612.39
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 citationPark, 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: 19761238
DOI: 10.1021/ja905640d
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237992

数据于2025-06-25公开中

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