scholarly journals Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly

2016 ◽  
Vol 25 (6) ◽  
pp. 1147-1155 ◽  
Author(s):  
Vladimir A. Meshcheryakov ◽  
Matthias Wolf
Keyword(s):  
Crystal Structure ◽  
Regulatory Role ◽  
Accessory Protein ◽  
Methanocaldococcus Jannaschii ◽  
Archaeal Flagellum

Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE″

2009 ◽  
Vol 76 (4) ◽  
pp. 787-793 ◽  
Author(s):  
Huihao Zhou ◽  
Qi Liu ◽  
Yongxiang Gao ◽  
Maikun Teng ◽  
Liwen Niu
Keyword(s):  
Crystal Structure ◽  
Methanocaldococcus Jannaschii

Crystal structure analysis of a hypothetical protein (MJ0366) from Methanocaldococcus jannaschii revealed a novel topological arrangement of the knot fold

2017 ◽  
Vol 482 (2) ◽  
pp. 264-269 ◽  
Author(s):  
Viswanathan Thiruselvam ◽  
Thirumananseri Kumarevel ◽  
Ponnuraj Karthe ◽  
Seiki Kuramitsu ◽  
Shigeyuki Yokoyama ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structure Analysis ◽  
Hypothetical Protein ◽  
Crystal Structure Analysis ◽  
Methanocaldococcus Jannaschii

scholarly journals Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori

2010 ◽  
Vol 78 (13) ◽  
pp. 2839-2848 ◽  
Author(s):  
Robert Lam ◽  
Vladimir Romanov ◽  
Kathy Johns ◽  
Kevin P. Battaile ◽  
Jean Wu-Brown ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Accessory Protein ◽  
Urease Accessory Protein

Leishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties

2000 ◽  
Vol 28 (2) ◽  
pp. 186-190 ◽  
Author(s):  
L. A. Fothergill-Gilmore ◽  
D. J. Rigden ◽  
P. A. M. Michels ◽  
S. E. V. Phillips
Keyword(s):  
Crystal Structure ◽  
Pyruvate Kinase ◽  
Regulatory Role ◽  
Structural Basis ◽  
Protozoan Parasites ◽  
Effector Molecule ◽  
T State ◽  
Regulatory Properties ◽  
Allosteric Activator

Glycolysis occupies a central role in cellular metabolism, and is of particular importance for the catabolic production of ATP in protozoan parasites such as Leishmania and Trypanosoma. In these organisms pyruvate kinase plays a key regulatory role, and is unique in responding to fructose 2,6-bisphosphate as allosteric activator. The determination of the crystal structure of the first eukaryotic pyruvate kinase in the T-state (the inactive or ‘tense’ conformation of allosteric enzymes) is described. A comparison of the effector sites of the Leishmania and yeast enzymes reveals the structural basis for the different effector specificity. Two loops, comprising residues 443–453 and 480–489, adopt very different conformations in the two enzymes, and Lys-453 and His-480 that are a feature of trypanosomatid enzymes provide probable ligands for the 2-phospho group of the effector molecule. These and other differences offer an opportunity for the design of drugs that would exploit regulatory differences between parasite and host.

scholarly journals Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein

PLoS ONE ◽  
2021 ◽  
Vol 16 (7) ◽  
pp. e0254232
Author(s):  
Van Son Nguyen ◽  
Silvia Spinelli ◽  
Éric Cascales ◽  
Alain Roussel ◽  
Christian Cambillau ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cell Wall ◽  
Protein Delivery ◽  
Cell Envelope ◽  
Interaction Network ◽  
Binding Domain ◽  
Target Cells ◽  
Accessory Protein ◽  
Type Vi Secretion System ◽  
Membrane Complex

The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved.

Structural Insight into the Interaction of Sendai Virus C Protein with Alix To Stimulate Viral Budding

2021 ◽  
Author(s):  
Kosuke Oda ◽  
Yasuyuki Matoba ◽  
Masanori Sugiyama ◽  
Takemasa Sakaguchi
Keyword(s):  
Crystal Structure ◽  
Binding Affinity ◽  
Sendai Virus ◽  
Antiviral Drugs ◽  
Accessory Protein ◽  
Type I ◽  
C Protein ◽  
Viral Budding ◽  
C Proteins

The Sendai virus (SeV), belonging to the Respirovirus genus of the family Paramyxoviridae , harbors an accessory protein, named C protein, which facilitates the viral pathogenicity in mice. In addition, the C protein is known to stimulate the budding of virus-like particles through the binding to the host ALG-2 interacting protein X (Alix), a component of the endosomal sorting complexes required for transport (ESCRT) machinery. However, siRNA-mediated gene knockdown studies suggested that neither Alix nor C protein are related to the SeV budding. In the present study, we determined the crystal structure of a complex comprising of the C -terminal half of the C protein (Y3) and the Bro1 domain of Alix at a resolution of 2.2 Å, to investigate the role of the association in the SeV budding. The structure revealed that a novel consensus sequence, LxxW, which is conserved among the Respirovirus C proteins, is important for the Alix-binding. SeV possessing a mutated C protein with a reduced Alix-binding affinity showed impaired virus production, which correlated with the binding affinity. Infectivity analysis showed a 160-fold reduction at 12 h post-infection compared with non-mutated virus, while C protein competes with CHMP4, one subunit of the ESCRT-III complex, on the binding to Alix. Altogether, these results highlight the critical role of C protein in the SeV budding. IMPORTANCE Human parainfluenza virus type I (hPIV1) is a respiratory pathogen affecting in young children, immunocompromised patients, and the elderly, with no available vaccines or antiviral drugs. Sendai virus (SeV), a murine counterpart of hPIV1, has been extensively studied to determine the molecular and biological properties of hPIV1. These viruses possess a multifunctional accessory protein, C protein, which is essential for stimulating the viral reproduction, however, its role in budding remains controversial. In the present study, the crystal structure of the C -terminal half of the SeV C protein associated with the Bro1 domain of Alix, a component of a cell membrane modulating machinery ESCRT, was elucidated. Based on the structure, we designed mutated C proteins with different binding affinity to Alix, and showed that the interaction between C and Alix is vital for the viral budding. These findings provide new insights into the development of a new antiviral drugs against hPIV1.

scholarly journals Crystal Structure of a Conserved Hypothetical Protein MJ0927 fromMethanocaldococcus jannaschiiReveals a Novel Quaternary Assembly in the Nif3 Family

2014 ◽  
Vol 2014 ◽  
pp. 1-8
Author(s):  
Sheng-Chia Chen ◽  
Chi-Hung Huang ◽  
Chia Shin Yang ◽  
Shu-Min Kuan ◽  
Ching-Ting Lin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Hypothetical Protein ◽  
Mobility Shift ◽  
Methanocaldococcus Jannaschii ◽  
Double Stranded Dna ◽  
Family Protein ◽  
Electrophoretic Mobility Shift Assays ◽  
Quaternary Assembly ◽  
Positively Charged

A Nif3 family protein ofMethanocaldococcus jannaschii, MJ0927, is highly conserved from bacteria to humans. Although several structures of bacterial Nif3 proteins are known, no structure representing archaeal Nif3 has yet been reported. The crystal structure ofMethanocaldococcus jannaschiiMJ0927 was determined at 2.47 Å resolution to understand the structural differences between the bacterial and archaeal Nif3 proteins. Intriguingly, MJ0927 is found to adopt an unusual assembly comprising a trimer of dimers that forms a cage-like architecture. Electrophoretic mobility-shift assays indicate that MJ0927 binds to both single-stranded and double-stranded DNA. Structural analysis of MJ0927 reveals a positively charged region that can potentially explain its DNA-binding capability. Taken together, these data suggest that MJ0927 adopts a novel quartenary architecture that could play various DNA-binding roles inMethanocaldococcus jannaschii.

Crystal Structure of Methanocaldococcus jannaschii Trm4 Complexed with Sinefungin

2010 ◽  
Vol 401 (3) ◽  
pp. 323-333 ◽  
Author(s):  
Mitsuo Kuratani ◽  
Masashi Hirano ◽  
Sakurako Goto-Ito ◽  
Yuzuru Itoh ◽  
Yasushi Hikida ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Methanocaldococcus Jannaschii
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