Structure of the UreD–UreF–UreG–UreE complex in Helicobacter pylori: a model study

Biagi, Francesco; Musiani, Francesco; Ciurli, Stefano

doi:10.1007/s00775-013-1002-8

Cited by 17 publications

(10 citation statements)

References 57 publications

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“…Previous modeling studies argued that UreF may serve as a GTPase-activating protein (GAP) based on sequence homology [41],[42]. Biagi et al generated a computational model of the UreE/UreG/UreF/UreH complex [42]. This model depicted UreG in an inverted orientation as compared to what was observed in the crystal structure of the UreG/UreF/UreH complex.…”

Section: Discussionmentioning

confidence: 99%

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

et al. 2013

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Section: Discussionmentioning

confidence: 99%

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

et al. 2013

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“…Although the interactions and mechanisms of action of these accessory proteins have been extensively studied and are known to be essential for urease maturation [30,52–63], the direct binding of a metallochaperone complex to the target apo-enzyme has yet not been demonstrated, perhaps due to the transient nature of the complex. However, there is a crystal structure of the H. pylori (UreHFG) 2 complex [30] and the complex with UreE has been modelled [56] (Figure 3). …”

Section: Metallochaperonesmentioning

confidence: 99%

“…( B ) H. pylori urease metallochaperone complex of UreD ( light blue ), UreF ( green ) and UreG ( grey ) (4hi0), including dimeric UreE ( orange ; 3yn0) in an orientation described in a previously reported docking model [56]. ( C ) The trimer-of-trimers urease apoprotein (UreA, UreB, UreC; cyan , 4z42) from Yersinia enterocolitica either sequentially binds UreD, UreF and UreG or binds a preformed UreD 2 F 2 G 2 complex.…”

Section: Figurementioning

confidence: 99%

Metallochaperones and metalloregulation in bacteria

Capdevila

Edmonds

Giedroc

2017

Essays in Biochemistry

111

117

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Bacterial transition metal homoeostasis or simply ‘metallostasis’ describes the process by which cells control the intracellular availability of functionally required metal cofactors, from manganese (Mn) to zinc (Zn), avoiding bothmetal deprivation and toxicity. Metallostasis is an emerging aspect of the vertebrate host–pathogen interface that is defined by a ‘tug-of-war’ for biologically essential metals and provides the motivation for much recent work in this area. The host employs a number of strategies to starve the microbial pathogen of essential metals, while for others attempts to limit bacterial infections by leveraging highly competitive metals. Bacteria must be capable of adapting to these efforts to remodel the transition metal landscape and employ highly specialized metal sensing transcriptional regulators, termed metalloregulatory proteins, and metallochaperones, that allocate metals to specific destinations, to mediate this adaptive response. In this essay, we discuss recent progress in our understanding of the structural mechanisms and metal specificity of this adaptive response, focusing on energy-requiring metallochaperones that play roles in the metallocofactor active site assembly in metalloenzymes and metallosensors, which govern the systems-level response to metal limitation and intoxication.

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“…Using Tandem Affinity Purification, we isolated from H. pylori cells a complex comprising UreA-B and the complete activation complex UreH-UreF-UreG-UreE (Stingl et al, 2008). A computational model of this complex was recently proposed (Biagi et al, 2013). …”

Section: In Vivo Urease Activation and Accessory Protein Complexesmentioning

confidence: 99%

Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pylori

Reuse

Vinella

Cavazza

2013

Front. Cell. Infect. Microbiol.

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Nickel is a virulence determinant for the human gastric pathogen Helicobacter pylori. Indeed, H. pylori possesses two nickel-enzymes that are essential for in vivo colonization, [NiFe] hydrogenase and urease, an abundant virulence factor that contains 24 nickel ions per active complex. Because of these two enzymes, survival of H. pylori relies on an important supply of nickel, implying a tight control of its distribution and storage. In this review, we will present the pathways of activation of the nickel enzymes as well as original mechanisms found in H. pylori for the uptake, trafficking and distribution of nickel between the two enzymes. These include (i) an outer-membrane nickel uptake system, the FrpB4 TonB-dependent transporter, (ii) overlapping protein complexes and interaction networks involved in nickel trafficking and distribution between urease and hydrogenase and, (iii) Helicobacter specific nickel-binding proteins that are involved in nickel storage and can play the role of metallo-chaperones. Finally, we will discuss the implication of the nickel trafficking partners in virulence and propose them as novel therapeutic targets for treatments against H. pylori infection.

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Structure of the UreD–UreF–UreG–UreE complex in Helicobacter pylori: a model study

Cited by 17 publications

References 57 publications

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

Metallochaperones and metalloregulation in bacteria

Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pylori

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