Results 111 to 120 of about 104,269 (134)

A conserved scaffold with heterogeneous metal ion binding site: the multifaceted example of HD-GYP proteins

Coordination Chemistry Reviews, 2022
Abstract The control of the intracellular level of cyclic dinucleotides is a major strategy to transduce external signals into a cellular response, particularly in bacteria. The HD-GYP metalloproteins, a subgroup of the larger family of histidine-aspartate (HD) hydrolases, can catalyze the cleavage of the phosphodiester bond(s) of cyclic ...
Francesca Cutruzzola, Alessandro Paiardini, Sharon Spizzichino   +2 more
exaly   +4 more sources

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The HD-GYP domain protein of Shewanella putrefaciens YZ08 regulates biofilm formation and spoilage activities

Food Research International, 2022
Shewanella putrefaciens is an important spoilage bacteria in seafood and its ability to form biofilms in food processing environments increases the chances of food spoilage. Exploring the regulatory factors associated with biofilm formation and spoilage activity in S. putrefaciens is of great significance for extending the shelf life of seafood.
Zhaoyang Ding, Jing Xie
exaly   +3 more sources

HD‐GYP domain proteins regulate biofilm formation and virulence in Pseudomonas aeruginosa

Environmental Microbiology, 2009
Summary HD‐GYP is a protein domain involved in the hydrolysis of the bacterial second messenger cyclic‐di‐GMP. The genome of the human pathogen Pseudomonas aeruginosa PAO1 encodes two proteins (PA4108, PA4781) with an HD‐GYP domain and a third protein, PA2572, which contains
Ryan, Robert P, Lucey, Jean, O'Donovan, Karen, McCarthy, Yvonne, Yang, Liang, Tolker-Nielsen, Tim, Dow, J Maxwell   +6 more
openaire   +4 more sources

Identification and Characterization of a Redox Sensor Phosphodiesterase from Ferrovum sp. PN-J185 Containing Bacterial Hemerythrin and HD-GYP Domains

Biochemistry, 2020
The second messenger bis(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates numerous important physiological functions in bacteria. In this study, we identified and characterized the first dimeric, full-length, non-heme iron-bound phosphodiesterase (PDE) containing bacterial hemerythrin and HD-GYP domains (Bhr-HD-GYP). We found that the
Kenichi Kitanishi, Jotaro Igarashi, Ariki Matsuoka, Masaki Unno   +3 more
openaire   +3 more sources

HD-GYP domain structure solved

Nature Reviews Microbiology, 2013
Sheilagh Molloy, Molloy Sheilagh
exaly   +2 more sources

Structure and Function of HD-GYP Phosphodiesterases

2020
HD-GYPs represent the least abundant, and somewhat mysterious, class of dedicated cyclic di-GMP phosphodiesterases (PDE). They are metal dependent enzymes, belonging to the HD phosphohydrolase superfamily, and are evolutionarily unrelated to the EAL class of cyclic di-GMP dedicated PDEs.
Rinaldo S., Paiardini A., Paone A., Cutruzzola' F., Giardina G.   +4 more
openaire   +2 more sources

Phenotypic–genotypic analysis of GGDEF/EAL/HD‐GYP domain‐encoding genes in Pseudomonas putida

Environmental Microbiology Reports, 2019
Summary Cyclic diguanylate (c‐di‐GMP) is a broadly conserved bacterial signalling molecule that modulates diverse cellular processes, such as biofilm formation, colony morphology and swimming motility. The intracellular level of c‐di‐GMP is controlled by diguanylate cyclases (DGCs) with GGDEF domain and ...
Hailing Nie, Yujie Xiao, Jinzhi He, Huizhong Liu, Liang Nie, Wenli Chen, Qiaoyun Huang   +6 more
openaire   +2 more sources

Characterization of GYP*Mur and novel GYP*Bun‐like hybrids in Thai blood donors reveals a qualitatively altered s antigen

Vox Sanguinis, 2020
Background and objectives: The Mi(a+) GP(B-A-B) hybrid phenotypes occur with a prevalence of 2%–23% across Southeast Asia. While the s antigen is alleged to be altered, no evidence for specific variants is known.
Philaiphon Jongruamklang, Shane Grimsley, Nicole Thornton   +2 more
exaly   +2 more sources

The HD-GYP Domain and Cyclic Di-GMP Signaling

2014
A role for the HD-GYP domain in c-di-GMP hydrolysis was then proposed based on examination of the distribution and numbers of GGDEF, EAL, and HD-GYP domains encoded by different bacterial genomes, coupled with the known activities of other members of the HD superfamily of enzymes as metal-dependent hydrolases.
Robert P. Ryan, Yvonne McCarthy, J. Maxwell Dow   +2 more
openaire   +1 more source

Cyclic di-GMP Signaling Gone Astray: Cyclic GAMP Signaling via Hypr GGDEF and HD-GYP Enzymes

2020
GGDEF domain and HD-GYP enzymes are classically associated with cyclic di-GMP signaling. Here we describe our current knowledge of variants of these enzyme classes that instead are involved in cyclic GMP-AMP (cGAMP) signaling, including their discovery, recent elucidation of signature active site residues, specific phenotypes, and regulatory mechanisms.
Todd A. Wright, Andrew B. Dippel, Ming C. Hammond   +2 more
openaire   +1 more source