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A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis

Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI_RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallizat...

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Autores principales: Trindade, Inês B., Fonseca, Bruno M., Matias, Pedro M., Louro, Ricardo O., Moe, Elin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5012204/
https://www.ncbi.nlm.nih.gov/pubmed/27599855
http://dx.doi.org/10.1107/S2053230X16011419
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author Trindade, Inês B.
Fonseca, Bruno M.
Matias, Pedro M.
Louro, Ricardo O.
Moe, Elin
author_facet Trindade, Inês B.
Fonseca, Bruno M.
Matias, Pedro M.
Louro, Ricardo O.
Moe, Elin
author_sort Trindade, Inês B.
collection PubMed
description Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI_RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 Å resolution. The SIP crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 48.04, b = 78.31, c = 67.71 Å, α = 90, β = 99.94, γ = 90°, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined ∼2 Å resolution SIP structures with ∼30% sequence identity as templates are ongoing.
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spelling pubmed-50122042016-09-14 A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis Trindade, Inês B. Fonseca, Bruno M. Matias, Pedro M. Louro, Ricardo O. Moe, Elin Acta Crystallogr F Struct Biol Commun Research Communications Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI_RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 Å resolution. The SIP crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 48.04, b = 78.31, c = 67.71 Å, α = 90, β = 99.94, γ = 90°, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined ∼2 Å resolution SIP structures with ∼30% sequence identity as templates are ongoing. International Union of Crystallography 2016-08-09 /pmc/articles/PMC5012204/ /pubmed/27599855 http://dx.doi.org/10.1107/S2053230X16011419 Text en © Trindade et al. 2016 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Communications
Trindade, Inês B.
Fonseca, Bruno M.
Matias, Pedro M.
Louro, Ricardo O.
Moe, Elin
A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis
title A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis
title_full A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis
title_fullStr A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis
title_full_unstemmed A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis
title_short A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis
title_sort putative siderophore-interacting protein from the marine bacterium shewanella frigidimarina ncimb 400: cloning, expression, purification, crystallization and x-ray diffraction analysis
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5012204/
https://www.ncbi.nlm.nih.gov/pubmed/27599855
http://dx.doi.org/10.1107/S2053230X16011419
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