The structural basis of transferrin sequestration by transferrin-binding protein B

Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin (Tf) during infection via a surface Tf receptor system composed of proteins TbpA and TbpB. Here in we present the crystal structures of TbpB from N. meningi...

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Autores principales: Calmettes, Charles, Alcantara, Joenel, Yu, Rong-Hua, Schryvers, Anthony B., Moraes, Trevor F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3981719/
https://www.ncbi.nlm.nih.gov/pubmed/22343719
http://dx.doi.org/10.1038/nsmb.2251
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author Calmettes, Charles
Alcantara, Joenel
Yu, Rong-Hua
Schryvers, Anthony B.
Moraes, Trevor F.
author_facet Calmettes, Charles
Alcantara, Joenel
Yu, Rong-Hua
Schryvers, Anthony B.
Moraes, Trevor F.
author_sort Calmettes, Charles
collection PubMed
description Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin (Tf) during infection via a surface Tf receptor system composed of proteins TbpA and TbpB. Here in we present the crystal structures of TbpB from N. meningitidis, in its apo form and in complex with human Tf (hTf). The structure reveals how TbpB sequesters hTf and initiates iron release from hTf.
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spelling pubmed-39817192014-04-09 The structural basis of transferrin sequestration by transferrin-binding protein B Calmettes, Charles Alcantara, Joenel Yu, Rong-Hua Schryvers, Anthony B. Moraes, Trevor F. Nat Struct Mol Biol Article Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin (Tf) during infection via a surface Tf receptor system composed of proteins TbpA and TbpB. Here in we present the crystal structures of TbpB from N. meningitidis, in its apo form and in complex with human Tf (hTf). The structure reveals how TbpB sequesters hTf and initiates iron release from hTf. 2012-02-19 /pmc/articles/PMC3981719/ /pubmed/22343719 http://dx.doi.org/10.1038/nsmb.2251 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Calmettes, Charles
Alcantara, Joenel
Yu, Rong-Hua
Schryvers, Anthony B.
Moraes, Trevor F.
The structural basis of transferrin sequestration by transferrin-binding protein B
title The structural basis of transferrin sequestration by transferrin-binding protein B
title_full The structural basis of transferrin sequestration by transferrin-binding protein B
title_fullStr The structural basis of transferrin sequestration by transferrin-binding protein B
title_full_unstemmed The structural basis of transferrin sequestration by transferrin-binding protein B
title_short The structural basis of transferrin sequestration by transferrin-binding protein B
title_sort structural basis of transferrin sequestration by transferrin-binding protein b
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3981719/
https://www.ncbi.nlm.nih.gov/pubmed/22343719
http://dx.doi.org/10.1038/nsmb.2251
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