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

被引:7
作者
Zhang, Ning [1 ]
Chang, Yong-Gang [1 ,7 ]
Tseng, Roger [1 ,6 ]
Ovchinnikov, Sergey [2 ]
Schwarz, Rakefet [4 ]
LiWang, Andy [1 ,3 ,5 ]
机构
[1] Univ Calif, Dept Chem & Chem Biol, Merced, CA 95343 USA
[2] Harvard Univ, Cambridge, MA 02138 USA
[3] Univ Calif, Ctr Cellular & Biomol Machines, Merced, CA USA
[4] Bar Ilan Univ, Mina & Everard Goodman Fac Life Sci, Ramat Gan, Israel
[5] Univ Calif, Hlth Sci Res Inst, Merced, CA USA
[6] USDA, Ames, IA USA
[7] Monash Univ, Clayton, Vic, Australia
基金
美国国家科学基金会;
关键词
biofilm; cyanobacteria; NMR spectroscopy; protein structure; S; elongatus PCC 7942; PHOTOTROPHIC BIOFILMS; COMMUNITY COMPOSITION; CHEMICAL-SHIFTS; SURFACE; EFFICIENT; BACKBONE; SOFTWARE; STONE;
D O I
10.1002/pro.3952
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 alpha+beta protein with alpha alpha beta beta beta beta alpha alpha topology and roll architecture, consisting of a four-stranded beta-sheet that is flanked by four alpha-helices on one side. Conserved surface residues constitute a hydrophobic pocket and charged regions that are likely also present in Se0862 orthologs.
引用
收藏
页码:2274 / 2280
页数:7
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