Crystal structure of ω transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 Å resolution 1 1Edited by R. Huber

2001 ◽  
Vol 314 (4) ◽  
pp. 789-796 ◽  
Author(s):  
Kazutaka Murayama ◽  
Peter Orth ◽  
Ana B de la Hoz ◽  
Juan C Alonso ◽  
Wolfram Saenger
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pyogenes ◽  
Transcriptional Repressor

scholarly journals Crystal structure of a phosphotransacetylase from Streptococcus pyogenes

2004 ◽  
Vol 55 (2) ◽  
pp. 479-481 ◽  
Author(s):  
Qian Steven Xu ◽  
Dong-Hae Shin ◽  
Ramona Pufan ◽  
Hisao Yokota ◽  
Rosalind Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pyogenes

scholarly journals Crystal Structure of Streptococcus pyogenes Cas1 and Its Interaction with Csn2 in the Type II CRISPR-Cas System

Structure ◽  
2016 ◽  
Vol 24 (1) ◽  
pp. 70-79 ◽  
Author(s):  
Donghyun Ka ◽  
Hasup Lee ◽  
Yi-Deun Jung ◽  
Kyunggon Kim ◽  
Chaok Seok ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pyogenes ◽  
Type Ii

Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes

2007 ◽  
Vol 68 (4) ◽  
pp. 1016-1019 ◽  
Author(s):  
Won-Ho Lee ◽  
Young Kwan Kim ◽  
Ki Hyun Nam ◽  
Amit Priyadarshi ◽  
Eun Hye Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Adenosine Deaminase ◽  
Streptococcus Pyogenes

scholarly journals Structural and Biochemical Studies of Dihydrofolate Reductase from Streptococcus pyogenes as a Target for Antifolate Antibiotics

2018 ◽  
Author(s):  
Behnoush Hajian ◽  
Jolanta Krucinska ◽  
Michael Martins ◽  
Narendran G-Dayanan ◽  
Kishore Viswanathan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pyogenes ◽  
Dihydrofolate Reductase ◽  
Wide Spectrum ◽  
Streptococcal Infections ◽  
Biochemical Studies ◽  
Live Bacteria ◽  
Dhfr Inhibitors ◽  
First Time ◽  
Structural Insights

ABSTRACTStreptococcus pyogenes, a beta-hemolytic bacterium, causes a wide spectrum of infections in human including pharyngitis, tonsillitis, scarlet fever, rheumatic fever, and necrotizing fasciitis. Streptococcal infections can also exist as co-infection with methicillin resistant Staphylococcus aureus (MRSA). Trimethoprim-sulfamethoxazole (TMP-SMX) combination has been used for treatment of S. pyogenes and MRSA co-infection. However, resistance to TMP, an inhibitor of dihydrofolate reductase enzyme (DHFR), has challenged the efficacy of TMP-SMX combination. We explored the activity of a series of novel DHFR inhibitors against S. pyogenes. This study identified potent inhibitors of DHFR enzyme from S. pyogenes with excellent inhibitory activity against the growth of the live bacteria. We determined, for the first time, the crystal structure of S. pyogenes DHFR which provides structural insights into design and development of antifolate agents against this global pathogen.

scholarly journals Crystal structure of Streptococcus pyogenes EndoS, an immunomodulatory endoglycosidase specific for human IgG antibodies

2014 ◽  
Vol 111 (18) ◽  
pp. 6714-6719 ◽  
Author(s):  
B. Trastoy ◽  
J. V. Lomino ◽  
B. G. Pierce ◽  
L. G. Carter ◽  
S. Gunther ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pyogenes ◽  
Igg Antibodies ◽  
Human Igg

Structural and functional characterization of the transcriptional repressor CsoR from Thermus thermophilus HB8

Microbiology ◽  
2010 ◽  
Vol 156 (7) ◽  
pp. 1993-2005 ◽  
Author(s):  
Keiko Sakamoto ◽  
Yoshihiro Agari ◽  
Kazuko Agari ◽  
Seiki Kuramitsu ◽  
Akeo Shinkai
Keyword(s):  
Crystal Structure ◽  
Metal Ion ◽  
Copper Ions ◽  
Thermus Thermophilus ◽  
Functional Characterization ◽  
Transcriptional Repressor ◽  
Binding Motif ◽  
Copper Binding ◽  
X Ray ◽  
Transcriptional Derepression

The TTHA1719 gene from Thermus thermophilus HB8 encodes an orthologue of the copper-sensing transcriptional repressor CsoR. X-ray crystal structure analysis of T. thermophilus CsoR indicated that it forms a homotetramer. The structures of the CsoR monomer and dimer are similar to those of Mycobacterium tuberculosis CsoR. In the absence of copper ions, T. thermophilus CsoR bound to the promoter region of the copper-sensitive operon copZ-csoR-copA, which encodes the copper chaperone CopZ, CsoR and the copper efflux P-type ATPase CopA, to repress their expression, while in the presence of approximately an equal amount of copper ion, CsoR was released from the DNA, to allow expression of the downstream genes. Both Cu(II) and Cu(I) ions could bind CsoR, and were effective for transcriptional derepression. Additionally, CsoR could also sense various other metal ions, such as Zn(II), Ag(I), Cd(II) and Ni(II), which led to transcriptional derepression. The copper-binding motif of T. thermophilus CsoR contains C-H-H, while those of most orthologues contain C-H-C. The X-ray crystal structure of T. thermophilus CsoR suggests that a histidine residue in the N-terminal domain is also involved in metal-ion binding; that is, the binding motif could be H-C-H-H, like that of Escherichia coli RcnR, which binds Ni(II)/Co(II). The non-conserved H70 residue in the metal-binding motif of T. thermophilus CsoR is important for its DNA-binding affinity and metal-ion responsiveness.

Model for Substrate Interactions in C5a Peptidase from Streptococcus pyogenes: A 1.9 Å Crystal Structure of the Active Form of ScpA

2009 ◽  
Vol 386 (3) ◽  
pp. 754-772 ◽  
Author(s):  
Todd F. Kagawa ◽  
Maurice R. O'Connell ◽  
Pania Mouat ◽  
Max Paoli ◽  
Paul W. O'Toole ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pyogenes ◽  
Active Form ◽  
Substrate Interactions

Crystallization and preliminary X-ray diffraction studies of Streptococcus pyogenes plasmid pSM19035-encoded ω transcriptional repressor

1999 ◽  
Vol 55 (12) ◽  
pp. 2041-2042 ◽  
Author(s):  
Kazutaka Murayama ◽  
Ana B. de la Hoz ◽  
Claudia Alings ◽  
Gema López ◽  
Peter Orth ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Transcriptional Repressor ◽  
Diffusion Method ◽  
Broad Host Range ◽  
X Rays ◽  
X Ray Diffraction ◽  
Crystal Forms ◽  
Space Group ◽  
Broad Host Range Plasmid ◽  
Peg 4000

The transcriptional repressor, ω protein, from the Streptococcus pyogenes broad-host-range plasmid pSM19035 was crystallized at pH 7.5 and 8.5 by the vapour-diffusion method using PEG 4000 as precipitant. Two crystal forms were obtained; the first belongs to the tetragonal space group P41212 or P43212 and the second to the hexagonal space group P61 or P65. The crystals are most likely to contain one ω protein in the asymmetric unit, with Vm values of 3.2 and 3.5 Å3 Da−1, respectively. The crystals diffract X-rays to 2.4 and 2.9 Å resolution for the tetragonal and hexagonal systems, respectively.

scholarly journals Crystal structure of the transcriptional repressor PagR of Bacillus anthracis

Microbiology ◽  
2010 ◽  
Vol 156 (2) ◽  
pp. 385-391 ◽  
Author(s):  
Haiyan Zhao ◽  
Arsen Volkov ◽  
Vidya Harini Veldore ◽  
James A. Hoch ◽  
Kottayil I. Varughese
Keyword(s):  
Crystal Structure ◽  
Bacillus Anthracis ◽  
Protein Sequence ◽  
Model Building ◽  
Protective Antigen ◽  
Transcriptional Repressor ◽  
Promoter Regions ◽  
Arsenate Resistance ◽  
Multi Wavelength ◽  
Direct Binding

PagR is a transcriptional repressor in Bacillus anthracis that controls the chromosomal S-layer genes eag and sap, and downregulates the protective antigen pagA gene by direct binding to their promoter regions. The PagR protein sequence is similar to those of members of the ArsR repressor family involved in the repression of arsenate-resistance genes in numerous bacteria. The crystal structure of PagR was solved using multi-wavelength anomalous diffraction (MAD) techniques and was refined with 1.8 å resolution diffraction data. The PagR molecules form dimers, as observed in all SmtB/ArsR repressor family proteins. In the crystal lattice four PagR dimers pack together to form an inactive octamer. Model-building studies suggest that the dimer binds to a DNA duplex with a bend of around 4 °.

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