1CJ5

BOVINE BETA-LACTOGLOBULIN A

Summary for 1CJ5

• Entry DOI: 10.2210/pdb1cj5/pdb
• Descriptor: BETA-LACTOGLOBULIN A (1 entity in total)
• Functional Keywords: beta-lactoglobulin a, dynamics, transport protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 18395.20

Authors

Kuwata, K.,Hoshino, M.,Forge, V.,Era, S.,Batt, C.A.,Goto, Y. (deposition date: 1999-04-22, release date: 2000-04-26, Last modification date: 2023-12-27)

Primary citation

Kuwata, K.,Hoshino, M.,Forge, V.,Era, S.,Batt, C.A.,Goto, Y.
Solution structure and dynamics of bovine beta-lactoglobulin A.
Protein Sci., 8:2541-2545, 1999

PubMed Abstract: Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel beta-barrel and one major alpha-helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including betaI-strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried under the major alpha-helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions.

PubMed: 10595563

Experimental method

SOLUTION NMR