Jessica K. Bell

University of San Diego

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Ellis Bell

University of San Diego

Joseph Provost

University of San Diego

David M. Segal

Meir Medical Center

Richard T. Marconi

Virginia Commonwealth University

J. Ellis Bell

Utrecht University

Daniel P. Miller

Virginia Commonwealth University

David R. Davies

National Institutes of Health

James Marion

GlaxoSmithKline (United States)

John V. McDowell

University of Kentucky

Janine Askins

National Cancer Institute

Cooperative Institutions

University of San Diego

Virginia Commonwealth University

National Institutes of Health

University of Richmond

Virginia Commonwealth University Medical Center

National Institute of Diabetes and Digestive and Kidney Diseases

Janssen (United States)

National Cancer Institute

University of Minnesota

University of Liverpool

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The Oligomeric Structure of Human Granzyme A Reveals the Molecular Determinants of Substrate Specificity

Jessica K. Bell David H. Goetz Sami Mahrus Jennifer L. Harris R.J. Fletterick

10.2210/pdb1orf/pdb

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Citations (0)

The enzymic processes in mammalian skeletal muscle

The Journal of Physiology (1928)

Myra K. Beattie Jessica K. Bell T. H́. Milroy

10.1113/jphysiol.1928.sp002465

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Citations (4)

Wiki Tool for Adaptive, Accesibility, Usability and Colaborative Hypermedia Courses: MediaWikiCourse

Lecture notes in computer science (2011)

Carlos de Castro Lozano Enrique García Salcines José Miguel Ramírez F. J. Burón Beatriz Sainz de Abajo

Adaptive hypermedia

10.1007/978-3-642-20810-2_3

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Citations (1)

Cyclic-di-GMP binding induces structural rearrangements in the PlzA and PlzC proteins of the Lyme disease and relapsing fever spirochetes: a possible switch mechanism for c-di-GMP-mediated effector functions

Pathogens and Disease (2016)

Katherine L. Mallory Daniel P. Miller Lee D. Oliver John C. Freedman Jessica L. Kostick-Dunn

The c-di-GMP network of Borrelia burgdorferi, a causative agent of Lyme disease, consists of Rrp1, a diguanylate cyclase/response regulator; Hpk1, a histidine kinase; PdeA and PdeB, c-di-GMP phosphodiesterases; and PlzA, a PilZ domain c-di-GMP receptor. Borrelia hermsii, a causative agent of tick-borne relapsing fever, possesses a putative c-di-GMP regulatory network that is uncharacterized. While B. burgdorferi requires c-di-GMP to survive within ticks, the associated effector mechanisms are poorly defined. Using site-directed mutagenesis, size exclusion chromatography, isothermal titration calorimetry and fluorescence resonance energy transfer, we investigate the interaction of c-di-GMP with the Borrelia PilZ domain-containing Plz proteins: B. burgdorferi PlzA and B. hermsii PlzC. The Plz proteins were determined to be monomeric in their apo and holo forms and to bind c-di-GMP with high affinity with a 1:1 stoichiometry. C-di-GMP binding induced structural rearrangements in PlzA and PlzC. C-di-GMP binding proved to be dependent on positive charge at R145 of the PilZ domain motif, R145xxxR. Comparative sequence analyses led to the identification of Borrelia consensus sequences for the PilZ domain signature motifs. This study provides insight into c-di-GMP:Plz receptor interaction and identifies a possible switch mechanism that may regulate Plz protein effector functions.

10.1093/femspd/ftw105

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Citations (21)

Analysis of the unique interaction of factor H with the periopathogen Treponema denticola: The paradox of factor H cleavage

Immunobiology (2012)

Daniel P. Miller John J. McDowell Jessica K. Bell J. Christopher Fenno Richard T. Marconi

Structural motif

10.1016/j.imbio.2012.08.029

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Biochemical and structural characterization of innate immunity kinase complex proteins

The FASEB Journal (2009)

R. Jason Call Rodolfo Ghirlando Jessica K. Bell

Protein‐protein interactions form the communication link from membrane bound receptors to their downstream cellular targets. Objective Our long‐term goal is to examine the protein‐protein interactions responsible for the activation and regulation of the Toll‐like receptor 3 (TLR3) signaling cascade that leads to type I interferon production. In the current study we have targeted the kinase scaffold proteins, TRAF family member‐associated NF‐κB activator (TANK) and NAK‐associated protein 1 (NAP1). Methods Bacterial expression systems have been used to produce recombinant target protein and refolding methods developed for insoluble targets. Initial biochemical characterization of recombinant targets was completed using circular dichroism (CD), gel filtration (GF) and analytical ultracentrifugation (AUC). Results The protein domain comprising the N‐terminal region of NAP1 can be successfully refolded as assessed by CD, while TANK is soluble. Both constructs form homo‐oligomers as determined by GF. AUC experiments show that the NAP1 N‐term behaves as an elongated dimer in vitro . Gel filtration studies of TANK's kinase interaction site show that it elutes as a dimer species. Conclusions The scaffold proteins, TANK and NAP1, form stable homo‐oligomers via their N‐terminal regions. Funding from the Am. Cancer Society (RJC) and supported in part by the NIH intramural research program, NIDDK (RG).

10.1096/fasebj.23.1_supplement.707.1

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The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity

Nature Structural & Molecular Biology (2003)

Jessica K. Bell David H. Goetz Sami Mahrus Jennifer L. Harris Robert J. Fletterick

Tetrapeptide

Saturated mutagenesis

Granzyme A

Tripeptide

10.1038/nsb944

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Citations (69)

Lateral Clustering of TLR3:dsRNA Signaling Units Revealed by TLR3ecd:3Fabs Quaternary Structure

Journal of Molecular Biology (2012)

Jinquan Luo Galina Obmolova T. Malia Sheng‐Jiun Wu Karen E. Duffy

TLR3

RNA Silencing

MDA5

Ectodomain

10.1016/j.jmb.2012.05.006

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Citations (44)

Structure of Treponema denticola Factor H Binding protein (FhbB), selenomethionine derivative

Daniel P. Miller John V. McDowell A. Héroux Jessica K. Bell Richard T. Marconi

Treponema denticola

Derivative (finance)

10.2210/pdb3qz0/pdb

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Crystallization of the factor H-binding protein, FhbB, from the periopathogenTreponema denticola

Acta Crystallographica Section F Structural Biology and Crystallization Communications (2011)

Daniel P. Miller John V. McDowell Jessica K. Bell Richard T. Marconi

Treponema denticola is a primary etiological agent of periodontal disease. T. denticola evades complement-mediated killing by binding to the host's factor H (FH), a negative regulator of the alternative complement pathway. The T. denticola FH-binding protein has been identified and designated as factor H-binding protein B (FhbB). Crystals of recombinant FhbB were obtained by the hanging-drop vapor-diffusion method using sodium citrate and 0.2 M sodium thiocyanate. FhbB crystals diffracted to 1.8 Å resolution and belonged to space group P43212 or P41212, with unit-cell parameters a = b = 46.76, c = 167.68 Å. Two FhbB molecules per asymmetric unit gave a Matthews coefficient of 2.2 Å3 Da−1 and a solvent content of 44%. FhbB is the smallest bacterially produced FH-binding protein identified to date. Determination of its structure will provide unique insight into the minimal structural determinants required for FH binding.

Treponema denticola

Thiocyanate

10.1107/s1744309111011298

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Citations (13)