Crystal Structures of the Receiver Domain of the Response Regulator PhoP from
            <i>Escherichia coli</i>
            in the Absence and Presence of the Phosphoryl Analog Beryllofluoride

Bachhawat, Priti; Stock, Ann

doi:10.1128/jb.00049-07

Cited by 75 publications

(111 citation statements)

References 54 publications

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“…This distance is similar to that observed for the PhoP/BeF 3 − complex. 27 Contacts from fluorine atoms include F1 to OG Thr83 and O Ile82, F2 to Lys106 NZ, and F3 to Mg 2 + . Mg 2 + is less well localised and is in a position different from its position in HupR WT N .…”

Section: Resultsmentioning

confidence: 99%

The HupR Receiver Domain Crystal Structure in its Nonphospho and Inhibitory Phospho States

Davies

Lowe

Vénien-Bryan

et al. 2009

Journal of Molecular Biology

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Section: Resultsmentioning

confidence: 99%

The HupR Receiver Domain Crystal Structure in its Nonphospho and Inhibitory Phospho States

Davies

Lowe

Vénien-Bryan

et al. 2009

Journal of Molecular Biology

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“…(However, some examples in which a few amino acid substitutions seem to be responsible for functional changes have also been reported (7,33).) The Salmonella and Yersinia PhoP proteins have 2 domains: a 120-residue N-terminal domain joined by a 5-residue linker to a 98-residue C-terminal domain (34). (The N-and C-terminal domains are 80.8% and 75.5% identical, respectively.)…”

Section: Discussionmentioning

confidence: 99%

Transcription factor function and promoter architecture govern the evolution of bacterial regulons

Pérez

Groisman

2009

Proc. Natl. Acad. Sci. U.S.A.

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Evolutionary changes in ancestral regulatory circuits can bring about phenotypic differences between related organisms. Studies of regulatory circuits in eukaryotes suggest that these modifications result primarily from changes in cis-regulatory elements (as opposed to alterations in the transcription factors that act upon these sequences). It is presently unclear how the evolution of gene regulatory circuits has proceeded in bacteria, given the rampant effects of horizontal gene transfer, which has significantly altered the composition of bacterial regulons. We now demonstrate that the evolution of the regulons governed by the regulatory protein PhoP in the related human pathogens Salmonella enterica and Yersinia pestis has entailed functional changes in the PhoP protein as well as in the architecture of PhoP-dependent promoters. These changes have resulted in orthologous PhoP proteins that differ both in their ability to promote transcription and in their role as virulence regulators. We posit that these changes allow bacterial transcription factors to incorporate newly acquired genes into ancestral regulatory circuits and yet retain control of the core members of a regulon.cis-regulatory elements ͉ horizontal gene transfer ͉ PhoP ͉ Salmonella ͉ Yersinia

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“…In the unphosphorylated RR, the side chain of Thr/Ser is oriented away from the phosphoacceptor, and that of Tyr/Phe extends outward toward the surface of the 4-5-5 face. Structures of activated receiver domains reveal that these side chains move in response to phosphorylation [36,37]. All activated receiver domains of the OmpR/PhoB subfamily form a symmetric dimer through the same interface involving 4-5-5.…”

Section: Receiver Domain Structuresmentioning

confidence: 99%

Bacterial Two-Component Systems: Structures and Signaling Mechanisms

Wang¹

2012

Protein Phosphorylation in Human Health

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Protein Phosphorylation in Human Health 440accepting chemotaxis proteins, and Phosphatases [1], hence the name. The HAMP domain connects TM2 to the dimerization and histidine phosphorylation domain (often abbreviated as DHp). A catalytic and ATP-binding (CA) domain lies at the carboxyl terminus. The combination of DHp and CA is sometimes referred to as the kinase domain. The TM helices, HAMP domains, and DHp domains are all involved in homodimerization. The sensor domain is likely to dimerize in the context of the entire protein. Sensor domains share little sequence identity, as is expected from their diverse functions of sensing various signals. However, available structures of sensor domains fall into a few common structural folds, suggesting conserved signal sensing mechanisms. The HAMP, DHp, and CA domains are common modules of HKs and have well conserved structures and sequences, especially DHp and CA, whose sequences contain several conserved motifs. There is an absolutely conserved histidine residue that is phosphorylated, and the phosphoryl group is then donated to an RR, in response to signals sensed by the sensor domain. How the sensor domain regulates the kinase activities is still unknown, due to the lack of full-length structures of the transmembrane sensor HKs. However, a large accumulation of structures of isolated domains in recent years has started to shed light on possible molecular mechanisms of the signal transduction. In this section, I will summarize these structures and discuss their conformational changes that transmit signals from the sensor domain to the kinase domain. Structures of sensor domainsSensor domains of histidine kinases are located in cytosol, in membrane, or outside of cell membrane (extracytosolic). Currently, there is little structural information of the membraneBacterial Two-Component Systems: Structures and Signaling Mechanisms 441 embedded sensor domains. The prototypical HK has an extracytosolic sensor domain that senses extracellular signals or conditions in the cell envelope. These sensor domains have highly diverse sequences. However, most of the known structures of extracytosolic sensor domains fall into three distinct structural folds, mixed , all-helical, and -sandwich. Unlike extracytosolic sensor domains, many cytosolic sensor domains can be annotated on the sequence level as PAS or GAF domains, which have related structural folds and are named from their occurrence in Period circadian, Aryl hydrocarbon receptor nuclear translocator, and Single-minded proteins (PAS) [2], or in cGMP-regulated cyclic nucleotide phosphodiesterases, Adenylate cyclases, and the bacterial transcriptional regulator FhlA (GAF) [3].

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Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog Beryllofluoride

Cited by 75 publications

References 54 publications

The HupR Receiver Domain Crystal Structure in its Nonphospho and Inhibitory Phospho States

The HupR Receiver Domain Crystal Structure in its Nonphospho and Inhibitory Phospho States

Transcription factor function and promoter architecture govern the evolution of bacterial regulons

Bacterial Two-Component Systems: Structures and Signaling Mechanisms

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