| Electrostatic properties of the anion selective porin Omp32 from Delftia acidovorans and of the arginine cluster of bacterial porins. | |
| | |
MedLine Citation:
|
PMID: 12021430 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
The functional properties of the anion-selective porin Omp32 from the bacterium Delftia acidovorans, formerly Comamonas acidovorans, are determined by the particularly narrow channel constriction and the electrostatic field inside and outside the pore. A cluster of arginines (Arg 38, Arg 75, and Arg 133) determines the electrostatic field close to the constriction zone. Stacked amino acids carrying charges are prone to drastic pK(a) shifts. However, optimized calculations of the titration behavior of charged groups, based on the finite-difference Poisson-Boltzmann technique, suggest that all the arginines are charged at physiological pH. Protonation of the clustered arginines is stabilized by one buried glutamate residue (Glu 58), which is strongly interacting with Arg 75 and Arg 38. This functional arrangement of three charged amino acid residues is of general significance because it is found in the constriction zones of all known 16-stranded porins from the alpha-, beta-, and gamma-proteobacteria. |
| | |
Authors:
|
Ulrich Zachariae; Assen Koumanov; Harald Engelhardt; Andrey Karshikoff |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Protein science : a publication of the Protein Society Volume: 11 ISSN: 0961-8368 ISO Abbreviation: Protein Sci. Publication Date: 2002 Jun |
Date Detail:
|
Created Date: 2002-05-21 Completed Date: 2003-07-29 Revised Date: 2009-11-18 |
Medline Journal Info:
|
Nlm Unique ID: 9211750 Medline TA: Protein Sci Country: United States |
Other Details:
|
Languages: eng Pagination: 1309-19 Citation Subset: IM |
Affiliation:
|
Abteilung Molekulare Strukturbiologie, Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Arginine / chemistry* Bacterial Proteins* Delftia acidovorans / chemistry* Hydrogen-Ion Concentration Models, Molecular Molecular Sequence Data Porins / chemistry* Protein Structure, Tertiary Proteobacteria / chemistry Sequence Alignment Static Electricity |
| Chemical | |
Reg. No./Substance:
|
0/Bacterial Proteins; 0/Omp32 protein, bacteria; 0/Porins; 74-79-3/Arginine |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry re...
Next Document: Conformational changes in chemically modified Escherichia coli thioredoxin monitored by H/D exchange...