气候变化领域集成服务门户(CCPortal): Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme

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DOI	10.1073/pnas.2100657118
	Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme
	Patterson D.C.; Ruiz M.P.; Yoon H.; Walker J.A.; Armache J.-P.; Yennawar N.H.; Weinert E.E.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:36
英文摘要	Cyclic dimeric guanosine monophosphate (c-di-GMP) serves as a second messenger that modulates bacterial cellular processes, including biofilm formation. While proteins containing both cdi- GMP synthesizing (GGDEF) and c-di-GMP hydrolyzing (EAL) domains are widely predicted in bacterial genomes, it is poorly understood how domains with opposing enzymatic activity are regulated within a single polypeptide. Herein, we report the characterization of a globin-coupled sensor protein (GCS) from Paenibacillus dendritiformis (DcpG) with bifunctional c-di-GMP enzymatic activity. DcpG contains a regulatory sensor globin domain linked to diguanylate cyclase (GGDEF) and phosphodiesterase (EAL) domains that are differentially regulated by gas binding to the heme; GGDEF domain activity is activated by the Fe(II)-NO state of the globin domain, while EAL domain activity is activated by the Fe(II)-O2 state. The in vitro activity of DcpG is mimicked in vivo by the biofilm formation of P. dendritiformis in response to gaseous environment, with nitric oxide conditions leading to the greatest amount of biofilm formation. The ability of DcpG to differentially control GGDEF and EAL domain activity in response to ligand binding is likely due to the unusual properties of the globin domain, including rapid ligand dissociation rates and high midpoint potentials. Using structural information from small-angle X-ray scattering and negative stain electron microscopy studies, we developed a structural model of DcpG, providing information about the regulatory mechanism. These studies provide information about full-length GCS protein architecture and insight into the mechanism by which a single regulatory domain can selectively control output domains with opposing enzymatic activities. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Bifunctional enzyme; Cyclic di-GMP; Heme sensor
语种	英语
scopus关键词	bifunctional enzyme; cyclic dimeric guanosine monophosphate; cyclic GMP; ferric oxide; globin coupled sensor protein; guanylate cyclase; hemoprotein; multifunctional enzyme; nitric oxide; oxygen; phosphodiesterase; unclassified drug; Article; biofilm; conformational transition; controlled study; dissociation; electron microscopy; enzyme activity; heme sensor signaling; ligand binding; nonhuman; Paenibacillus; Paenibacillus dendritiformis; protein domain; signal transduction; X ray crystallography
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/238406
作者单位	Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, United States; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, United States; Department of Chemistry, Emory University, Atlanta, GA 30322, United States; The Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802, United States
推荐引用方式 GB/T 7714	Patterson D.C.,Ruiz M.P.,Yoon H.,et al. Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme[J],2021,118(36).
APA	Patterson D.C..,Ruiz M.P..,Yoon H..,Walker J.A..,Armache J.-P..,...&Weinert E.E..(2021).Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme.Proceedings of the National Academy of Sciences of the United States of America,118(36).
MLA	Patterson D.C.,et al."Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme".Proceedings of the National Academy of Sciences of the United States of America 118.36(2021).