Highlighting membrane protein structure and function: A celebration of the Protein Data Bank

Authors

Fei Li, University of California, San Francisco
Pascal F. Egea, University of California Los Angeles
Alex J. Vecchio, University of Nebraska-LincolnFollow
Ignacio Asial, DotBio Pte. Ltd
Meghna Gupta, University of California, San Francisco
Joana Paulino, University of California, San Francisco
Ruchika Bajaj, University of California, San Francisco
Miles Sasha Dickinson, University of California, San Francisco
Shelagh Fergunson-Miller, Michigan State University
Brian C. Monk, University of Otago
Robert M. Stroud, University of California, San Francisco

ORCID IDs

Pascal F. Egea

Meghna Gupta

Joana Paulino

Miles Sasha Dickinson

Shelagh Ferguson-Miller

Robert M. Stroud

Document Type

Article

Date of this Version

3-18-2021

Citation

J. Biol. Chem. (2021) 296 100557 https://doi.org/10.1016/j.jbc.2021.100557

Comments

CC-BY

Abstract

Biological membranes define the boundaries of cells and compartmentalize the chemical and physical processes required for life. Many biological processes are carried out by proteins embedded in or associated with such membranes. Determination of membrane protein (MP) structures at atomic or near-atomic resolution plays a vital role in elucidating their structural and functional impact in biology. This endeavor has determined 1198 unique MP structures as of early 2021. The value of these structures is expanded greatly by deposition of their three-dimensional (3D) coordinates into the Protein Data Bank (PDB) after the first atomic MP structure was elucidated in 1985. Since then, free access to MP structures facilitates broader and deeper understanding of MPs, which provides crucial new insights into their biological functions. Here we highlight the structural and functional biology of representative MPs and landmarks in the evolution of new technologies, with insights into key developments influenced by the PDB in magnifying their impact.