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

Fei Li; Pascal F Egea; Alex J Vecchio; Ignacio Asial; Meghna Gupta; Joana Paulino; Ruchika Bajaj; Miles Sasha Dickinson; Shelagh Ferguson-Miller; Brian C Monk; Robert M Stroud

doi:10.1016/j.jbc.2021.100557

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

J Biol Chem. 2021 Jan-Jun:296:100557. doi: 10.1016/j.jbc.2021.100557. Epub 2021 Mar 18.

Authors

Affiliations

¹ Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA; Department of Neurology, University of California San Francisco, San Francisco, California, USA.
² Department of Biological Chemistry, School of Medicine, University of California Los Angeles, Los Angeles, California, USA.
³ Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA.
⁴ DotBio Pte. Ltd, Singapore, Singapore.
⁵ Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA.
⁶ Department of Bioengineering and Therapeutic Sciences, University of California San Francisco, San Francisco, California, USA.
⁷ Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.
⁸ Sir John Walsh Research Institute and Department of Oral Sciences, University of Otago, North Dunedin, Dunedin, New Zealand.
⁹ Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA. Electronic address: stroud@msg.ucsf.edu.

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.

Keywords: bioenergetics; channel; drug discovery; lipid mimetics; membrane protein; membrane protein biogenesis; protein design; receptor; structure-function; transmembrane transport.

Publication types

Historical Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

MeSH terms

Databases, Protein* / history
History, 20th Century
History, 21st Century
Membrane Proteins / chemistry*
Membrane Proteins / metabolism*
Protein Conformation
Structure-Activity Relationship

Substances

Membrane Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding