Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens

Hammerschmid, Dietmar; Germani, Francesca; Drusin, Salvador Iván; Fagnen, Charline; Schuster, Claudio D.; Hoogewijs, David; Martí, Marcelo A.; Vénien-Bryan, Catherine; Moëns, Luc; Doorslaer, Sabine Van; Sobott, Frank; Dewilde, Sylvia

doi:10.1016/j.csbj.2021.03.031

Cited by 2 publications

References 105 publications

(143 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

Bacterial Oxygen Sensing by Globin‐Coupled Sensor Proteins

Hoque,

Weinert

2024

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

Organisms adapt to fluctuating oxygen levels using a variety of strategies, including coupling sensory domains to regulatory functions that modulate physiology and phenotypes. Globin‐coupled sensor proteins are multidomain proteins composed of a heme‐containing globin domain associated with a range of output domains, ranging from methyl‐accepting chemotaxis proteins, kinases, and diguanylate cyclases. These proteins have been found in the genomes of many bacteria, indicating their involvement in regulating diverse cellular pathways and behaviors in response to gaseous ligands. Detailed characterizations of globin‐coupled sensors have utilized a wide array of biochemical and spectroscopic methods to understand ligand binding and signal transduction in the heme domain. The diversity of the globin‐coupled sensory family studied to date highlights unique ligand‐binding characteristics in the heme pocket. While the characterization of the globin‐coupled sensor family has elucidated the mechanisms by which oxygen binds the heme moiety and influences the activity of these sensor protein output domains, the downstream proteins and pathways governed by globin‐coupled sensor signaling are not well understood. Given the breadth of the globin‐coupled sensors studied to date, additional research is needed further to elucidate the role of globin‐coupled sensor proteins in managing oxygen‐dependent microbial physiology both in vitro and in vivo.

show abstract

Bacterial Oxygen Sensing by Globin‐Coupled Sensor Proteins

Hoque,

Weinert

2024

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

show abstract

Signal transduction mechanisms in heme-based globin-coupled oxygen sensors with a focus on a histidine kinase (AfGcHK) and a diguanylate cyclase (YddV or EcDosC)

Vávra

Sergunin

Jeřábek

et al. 2022

Biological Chemistry

View full text Add to dashboard Cite

Heme is a vital cofactor of proteins with roles in oxygen transport (e.g. hemoglobin), storage (e.g. myoglobin), and activation (e.g. P450) as well as electron transfer (e.g. cytochromes) and many other functions. However, its structural and functional role in oxygen sensing proteins differs markedly from that in most other enzymes, where it serves as a catalytic or functional center. This minireview discusses the mechanism of signal transduction in two heme-based oxygen sensors: the histidine kinase AfGcHK and the diguanylate cyclase YddV (EcDosC), both of which feature a heme-binding domain containing a globin fold resembling that of hemoglobin and myoglobin.

show abstract

Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens

Abstract: Graphical abstract

Cited by 2 publications

References 105 publications

Bacterial Oxygen Sensing by Globin‐Coupled Sensor Proteins

Bacterial Oxygen Sensing by Globin‐Coupled Sensor Proteins

Signal transduction mechanisms in heme-based globin-coupled oxygen sensors with a focus on a histidine kinase (AfGcHK) and a diguanylate cyclase (YddV or EcDosC)

Contact Info

Product

Resources

About