bioRxivBioinformaticsPreprint
Quaternary structure evaluation tool for protein assemblies
Selçuk KorkmaziD, José M. DuarteiD, Andreas PrlićiD, Dinçer GöksülükiD, Gökmen ZararsıziD, Osman SaraçbaşıiD, Stephen Kevin BurleyiD, Peter W. RoseiD
Abstract
The Protein Data Bank (PDB) is the single worldwide archive of experimentally-determined three-dimensional (3D) structures of proteins and nucleic acids. As of January 2017, the PDB housed more than 125,000 structures and was growing by more than 11,000 structures annually. Since the 3D structure of a protein is vital to understand the mechanisms of biological processes, diseases, and drug design, correct oligomeric assembly information is of critical importance. For example, it makes a difference if the protein is normally a dimer and not a monomer or a trimer or a tetramer or a hexamer in nature. Unfortunately, the biologically relevant oligomeric form of a 3D structure is not directly obtainable by X-ray crystallography. Instead, this information may be provided by the PDB Depositor as metadata coming from additional experiments, be inferred by sequence-sequence comparisons with similar proteins of known oligomeric state, or predicted using software, such as PISA (Proteins, Interfaces, Structures and Assemblies) or EPPIC (Evolutionary Protein Protein Interface Classifier). Despite significant efforts by professional PDB Biocurators during data deposition, there remain a number of structures in the archive with incorrect quaternary structure descriptions (or annotations). Further investigation is, therefore, needed to evaluate the correctness of quaternary structure annotations. In this study, we aim to identify the most probable oligomeric states for proteins represented in the PDB. Our approach evaluated the performance of four independent prediction methods, including text mining of primary publications, inference from homologous protein structures, and two computational methods (PISA and EPPIC). Aggregating predictions to give consensus results outperformed all four of the independent prediction methods, yielding 86% correct, 9% incorrect, and 5% inconclusive predictions, when tested with a well-curated benchmark dataset. We have developed a freely-available web-based tool to make this approach accessible to researchers and PDB Biocurators (http://quatstruct.rcsb.org).
- Citations
- 1
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Automated evaluation of quaternary structures from protein crystals
Spencer E. Bliven, Aleix Lafita, … José M. Duarte·PLoS Computational BiologyPeer-reviewed·Apr 30, 2018
- Protein Quaternary Structures in Solution are a Mixture of Multiple forms
S. Marciano, D. Debabrata, … G. Schreiber·bioRxiv·Mar 30, 2022
- When can AlphaFold predict the oligomeric states of proteins?
Yiechang Lin, Ciara Wallis, Ben Corry·Protein SciencePeer-reviewed·Jun 16, 2026
- Principles and characteristics of biological assemblies in experimentally determined protein structures
Qifang Xu, Roland L. Dunbrack·Current Opinion in Structural BiologyPeer-reviewed·Apr 1, 2019
- The Protein Common Assembly Database (ProtCAD): A comprehensive structural resource of protein complexes
Qifang Xu, Roland L. Dunbrack·Nucleic Acids ResearchPeer-reviewed·Oct 11, 2022
- Protein language models can capture protein quaternary state
Orly Avraham, Tomer Tsaban, … Ora Schueler‐Furman·BMC BioinformaticsPeer-reviewed·Nov 14, 2023