Crystal Structures of Two Solute Receptors for l-Cystine and l-Cysteine, Respectively, of the Human Pathogen Neisseria gonorrhoeae

2012 ◽  
Vol 415 (3) ◽  
pp. 560-572 ◽  
Author(s):  
Haydar Bulut ◽  
Sebastien Moniot ◽  
Anke Licht ◽  
Frank Scheffel ◽  
Stephanie Gathmann ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Crystal Structures ◽  
Human Pathogen

scholarly journals Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Sara Pintar ◽  
Jure Borišek ◽  
Aleksandra Usenik ◽  
Andrej Perdih ◽  
Dušan Turk
Keyword(s):  
Crystal Structures ◽  
Active Site ◽  
Drug Targets ◽  
Substrate Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Human Pathogen ◽  
Active Site Cleft ◽  
Novel Drug ◽  
Novel Drug Targets

AbstractTo achieve productive binding, enzymes and substrates must align their geometries to complement each other along an entire substrate binding site, which may require enzyme flexibility. In pursuit of novel drug targets for the human pathogen S. aureus, we studied peptidoglycan N-acetylglucosaminidases, whose structures are composed of two domains forming a V-shaped active site cleft. Combined insights from crystal structures supported by site-directed mutagenesis, modeling, and molecular dynamics enabled us to elucidate the substrate binding mechanism of SagB and AtlA-gl. This mechanism requires domain sliding from the open form observed in their crystal structures, leading to polysaccharide substrate binding in the closed form, which can enzymatically process the bound substrate. We suggest that these two hydrolases must exhibit unusual extents of flexibility to cleave the rigid structure of a bacterial cell wall.

Different responses to nitrate and nitrite by the model organism Escherichia coli and the human pathogen Neisseria gonorrhoeae

2006 ◽  
Vol 34 (1) ◽  
pp. 111-114 ◽  
Author(s):  
R.N. Whitehead ◽  
J.A. Cole
Keyword(s):  
Escherichia Coli ◽  
Neisseria Gonorrhoeae ◽  
Model Organism ◽  
Anaerobic Growth ◽  
Human Pathogen ◽  
Regulate Gene Expression ◽  
E Coli ◽  
Regulatory Systems ◽  
Two Component ◽  
Nitrate And Nitrite

The ability of Escherichia coli to use both nitrate and nitrite as terminal electron acceptors during anaerobic growth is mediated by the dual-acting two-component regulatory systems NarX-NarL and NarQ-NarP. In contrast, Neisseria gonorrhoeae responds only to nitrite: it expresses only NarQ-NarP. We have shown that although N. gonorrhoeae NarQ can phosphorylate E. coli NarL and NarP, the N. gonorrhoeae NarP is unable to regulate gene expression in E. coli. Mutagenesis experiments have revealed residues in E. coli NarQ that are essential for nitrate and nitrite sensing. Chimaeric proteins revealed domains of NarQ that are important for ligand sensing.

scholarly journals Complete Genome Sequence of Neisseria gonorrhoeae NCCP11945

2008 ◽  
Vol 190 (17) ◽  
pp. 6035-6036 ◽  
Author(s):  
Gyung Tae Chung ◽  
Jeong Sik Yoo ◽  
Hee Bok Oh ◽  
Yeong Seon Lee ◽  
Sun Ho Cha ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Neisseria Gonorrhoeae ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Multidrug Resistant ◽  
Human Pathogen ◽  
Korean Patient

ABSTRACT Neisseria gonorrhoeae is an obligate human pathogen that is the etiological agent of gonorrhea. We explored variations in the genes of a multidrug-resistant N. gonorrhoeae isolate from a Korean patient in an effort to understand the prevalence, antibiotic resistance, and importance of horizontal gene transfer within this important, naturally competent organism. Here, we report the complete annotated genome sequence of N. gonorrhoeae strain NCCP11945.

Species specificity of factor H interaction with the uniquely human pathogen, Neisseria gonorrhoeae, resides in arginine substitution at position 1203 in domain 20

2010 ◽  
Vol 47 (13) ◽  
pp. 2247-2247
Author(s):  
Jutamas Shaughnessy ◽  
Sanjay Ram ◽  
Arnab Bhattacharjee ◽  
Connie Tran ◽  
Gabor Horvath ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Factor H ◽  
Species Specificity ◽  
Human Pathogen

scholarly journals Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae

2009 ◽  
Vol 106 (11) ◽  
pp. 4447-4452 ◽  
Author(s):  
A. Vik ◽  
F. E. Aas ◽  
J. H. Anonsen ◽  
S. Bilsborough ◽  
A. Schneider ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Broad Spectrum ◽  
Protein Glycosylation ◽  
Human Pathogen

scholarly journals Regulation of mtrF Expression in Neisseria gonorrhoeae and Its Role in High-Level Antimicrobial Resistance

2005 ◽  
Vol 187 (11) ◽  
pp. 3713-3720 ◽  
Author(s):  
Jason P. Folster ◽  
William M. Shafer
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Antimicrobial Agents ◽  
Efflux Pump ◽  
Sublethal Concentration ◽  
Human Pathogen ◽  
Mucosal Surfaces ◽  
Induction Process ◽  
Inner Membrane Protein ◽  
High Level ◽  
Triton X

ABSTRACT The obligate human pathogen Neisseria gonorrhoeae uses the MtrC-MtrD-MtrE efflux pump to resist structurally diverse hydrophobic antimicrobial agents (HAs), some of which bathe mucosal surfaces that become infected during transmission of gonococci. Constitutive high-level HA resistance occurs by the loss of a repressor (MtrR) that negatively controls transcription of the mtrCDE operon. This high-level HA resistance also requires the product of the mtrF gene, which is located downstream and transcriptionally divergent from mtrCDE. MtrF is a putative inner membrane protein, but its role in HA resistance mediated by the MtrC-MtrD-MtrE efflux pump remains to be determined. High-level HA resistance can also be mediated through an induction process that requires enhanced transcription of mtrCDE when gonococci are grown in the presence of a sublethal concentration of Triton X-100. We now report that inactivation of mtrF results in a significant reduction in the induction of HA resistance and that the expression of mtrF is enhanced when gonococci are grown under inducing conditions. However, no effect was observed on the induction of mtrCDE expression in an MtrF-negative strain. The expression of mtrF was repressed by MtrR, the major repressor of mtrCDE expression. In addition to MtrR, another repressor (MpeR) can downregulate the expression of mtrF. Repression of mtrF by MtrR and MpeR was additive, demonstrating that the repressive effects mediated by these regulators are independent processes.

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