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Plos One : a 3-dimensional Trimeric B-barrel Model for Chlamydia Momp Contains Conserved and Novel Elements of Gram- Negative Bacterial Porins, Volume 8

By Motta, Andrea

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Book Id: WPLBN0003942493
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos One : a 3-dimensional Trimeric B-barrel Model for Chlamydia Momp Contains Conserved and Novel Elements of Gram- Negative Bacterial Porins, Volume 8  
Author: Motta, Andrea
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection
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Publisher: Plos

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Motta, A. (n.d.). Plos One : a 3-dimensional Trimeric B-barrel Model for Chlamydia Momp Contains Conserved and Novel Elements of Gram- Negative Bacterial Porins, Volume 8. Retrieved from http://www.ebooklibrary.org/


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Description : Chlamydia trachomatis is the most prevalent cause of bacterial sexually transmitted diseases and the leading cause of preventable blindness worldwide. Global control of Chlamydia will best be achieved with a vaccine, a primary target for which is the major outer membrane protein, MOMP, which comprises ,60% of the outer membrane protein mass of this bacterium. In the absence of experimental structural information on MOMP, three previously published topology models presumed a16-stranded barrel architecture. Here, we use the latest b-barrel prediction algorithms, previous 2D topology modeling results, and comparative modeling methodology to build a 3D model based on the 16-stranded, trimeric assumption. We find that while a 3D MOMP model captures many structural hallmarks of a trimeric 16-stranded b-barrel porin, and is consistent with most of the experimental evidence for MOMP, MOMP residues 320–334 cannot be modeled as b-strands that span the entire membrane, as is consistently observed in published 16-stranded b-barrel crystal structures. Given the ambiguous results for b-strand delineation found in this study, recent publications of membrane b-barrel structures breaking with the canonical rule for an even number of b-strands, findings of b-barrels with strand-exchanged oligomeric conformations, and alternate folds dependent upon the lifecycle of the bacterium, we suggest that although the MOMP porin structure incorporates canonical 16-stranded conformations, it may have novel oligomeric or dynamic structural changes accounting for the discrepancies observed.

 

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