Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation

Ning Zhang, Yong Gang Chang, Roger Tseng, Sergey Ovchinnikov, Rakefet Schwarz, Andy LiWang

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and involved in regulation of biofilm formation in the cyanobacterium Synechococcus elongatus PCC 7942. Se0862 is a class α+β protein with ααββββαα topology and roll architecture, consisting of a four-stranded β-sheet that is flanked by four α-helices on one side. Conserved surface residues constitute a hydrophobic pocket and charged regions that are likely also present in Se0862 orthologs.

Original languageEnglish
Pages (from-to)2274-2280
Number of pages7
JournalProtein Science
Volume29
Issue number11
DOIs
StatePublished - 1 Nov 2020

Bibliographical note

Publisher Copyright:
© 2020 The Protein Society

Funding

This research was supported by grants from Air Force Office of Scientific Research (FA9550‐17‐1‐0447) and NSF‐CREST: Center for Cellular and Biomolecular Machines at the University of California, Merced (NSF‐HRD‐1547848). Molecular graphics and analyses performed with UCSF ChimeraX, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from National Institutes of Health R01‐GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases. This research was supported by grants from Air Force Office of Scientific Research (FA9550-17-1-0447) and NSF-CREST: Center for Cellular and Biomolecular Machines at the University of California, Merced (NSF-HRD-1547848). Molecular graphics and analyses performed with UCSF ChimeraX, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.

FundersFunder number
NSF-CREST
NSF‐CRESTNSF‐HRD‐1547848
National Institutes of Health
National Institute of General Medical SciencesR01GM129325
National Institute of Allergy and Infectious Diseases
Air Force Office of Scientific ResearchFA9550‐17‐1‐0447

    Keywords

    • NMR spectroscopy
    • S. elongatus PCC 7942
    • biofilm
    • cyanobacteria
    • protein structure

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