[NMR paper] Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA
FapA is an accessory protein within the biofilm forming functional bacterial amyloid related fap-operon in Pseudomonas, and maybe a chaperone for FapC controlling its fibrillization. To allow further structural analysis, here we present a complete sequential assignment of ¹H(amide), ^(13)C(?), ^(13)C(?), and ^(15)N NMR resonances for the functional form of the monomeric soluble FapA protein, comprising amino acids between 29 and 152. From these observed chemical shifts, the secondary structure...
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
ABSTRACT
Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and...
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09-21-2020 05:44 PM
[NMR paper] Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
Protein Sci. 2020 Sep 18;:
Authors: Zhang N, Chang YG, Tseng R, Ovchinnikov S, Schwarz R, LiWang A
Abstract
Biofilms are accumulations of microorganisms embedded in...
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[ASAP] Staphylococcus aureus Glucose-Induced Biofilm Accessory Protein A (GbaA) Is a Monothiol-Dependent Electrophile Sensor
Staphylococcus aureus Glucose-Induced Biofilm Accessory Protein A (GbaA) Is a Monothiol-Dependent Electrophile Sensor
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00347/20200729/images/medium/bi0c00347_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00347
http://feeds.feedburner.com/~r/acs/bichaw/~4/aVvLgIVQo9U
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07-30-2020 05:28 PM
[NMR paper] Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Related Articles Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Proc Natl Acad Sci U S A. 2016 Jun 13;
Authors: Shu Q, Krezel AM, Cusumano ZT, Pinkner JS, Klein R, Hultgren SJ, Frieden C
Abstract
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of...
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06-15-2016 11:12 PM
[NMR paper] Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from E. coli.
Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from E. coli.
Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from E. coli.
J Biol Chem. 2014 Jun 23;
Authors: Eichmann C, Tzitzilonis C, Bordignon E, Maslennikov I, Choe S, Riek R
Abstract
The solution NMR structure of the ?-helical integral membrane protein YgaP from Escherichia coli in mixed DHPC-7/LMPG micelles is presented. In these micelles, YgaP forms a homo-dimer with the two transmembrane helices...
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06-25-2014 08:06 PM
[NMR paper] Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Related Articles Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Structure. 2014 May 14;
Authors: Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific...
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05-20-2014 11:10 PM
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Publication date: Available online 15 May 2014
Source:Structure</br>
Author(s): Alessandro*A. Rizzo , Margaret*M. Suhanovsky , Matthew*L. Baker , LaTasha*C.R. Fraser , Lisa*M. Jones , Don*L. Rempel , Michael*L. Gross , Wah Chiu , Andrei*T. Alexandrescu , Carolyn*M. Teschke</br>
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique...
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05-15-2014 07:23 PM
[NMR paper] Assignment and secondary-structure determination of monomeric bovine seminal ribonucl
Assignment and secondary-structure determination of monomeric bovine seminal ribonuclease employing computer-assisted evaluation of homonuclear three-dimensional 1H-NMR spectra.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Assignment and secondary-structure determination of monomeric bovine seminal ribonuclease employing computer-assisted evaluation of homonuclear three-dimensional 1H-NMR spectra.
Eur J Biochem. 1995 Apr 15;229(2):494-502
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Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA
Linear Mode
