Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774

Bibliographic Details
Main Author: Gavel, Olga Yu
Publication Date: 2008
Other Authors: Kladova, Anna V., Bursakov, Sergey A., Dias, João M., Texeira, Susana, Shnyrov, Valery L., Moura, José J. G., Moura, Isabel, Romão, Maria J., Trincão, José
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: https://doi.org/10.1107/S1744309108008816
Summary: Native zinc/cobalt-containing ATP sulfurylase (ATPS; EC 2.7.7.4; MgATP:sulfate adenylyltransferase) from Desulfovibrio desulfuricans ATCC 27774 was purified to homogeneity and crystallized. The orthorhombic crystals diffracted to beyond 2.5 Å resolution and the X-ray data collected should allow the determination of the structure of the zinc-bound form of this ATPS. Although previous biochemical studies of this protein indicated the presence of a homotrimer in solution, a dimer was found in the asymmetric unit. Elucidation of this structure will permit a better understanding of the role of the metal in the activity and stability of this family of enzymes.
id RCAP_76dea9ca7d3040b847de25f583bbd96d
oai_identifier_str oai:run.unl.pt:10362/62998
network_acronym_str RCAP
network_name_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository_id_str https://opendoar.ac.uk/repository/7160
spelling Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774ATP sulfurylasesCobaltSulfate-reducing bacteriaZincBiophysicsStructural BiologyBiochemistryGeneticsCondensed Matter PhysicsNative zinc/cobalt-containing ATP sulfurylase (ATPS; EC 2.7.7.4; MgATP:sulfate adenylyltransferase) from Desulfovibrio desulfuricans ATCC 27774 was purified to homogeneity and crystallized. The orthorhombic crystals diffracted to beyond 2.5 Å resolution and the X-ray data collected should allow the determination of the structure of the zinc-bound form of this ATPS. Although previous biochemical studies of this protein indicated the presence of a homotrimer in solution, a dimer was found in the asymmetric unit. Elucidation of this structure will permit a better understanding of the role of the metal in the activity and stability of this family of enzymes.CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)DQ - Departamento de QuímicaRUNGavel, Olga YuKladova, Anna V.Bursakov, Sergey A.Dias, João M.Texeira, SusanaShnyrov, Valery L.Moura, José J. G.Moura, IsabelRomão, Maria J.Trincão, José2019-03-11T23:15:26Z2008-01-012008-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article3application/pdfhttps://doi.org/10.1107/S1744309108008816eng1744-3091PURE: 12013158http://www.scopus.com/inward/record.url?scp=46949100709&partnerID=8YFLogxKhttps://doi.org/10.1107/S1744309108008816info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-22T17:37:40Zoai:run.unl.pt:10362/62998Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T17:08:36.705712Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
title Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
spellingShingle Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
Gavel, Olga Yu
ATP sulfurylases
Cobalt
Sulfate-reducing bacteria
Zinc
Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
title_short Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
title_full Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
title_fullStr Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
title_full_unstemmed Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
title_sort Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
author Gavel, Olga Yu
author_facet Gavel, Olga Yu
Kladova, Anna V.
Bursakov, Sergey A.
Dias, João M.
Texeira, Susana
Shnyrov, Valery L.
Moura, José J. G.
Moura, Isabel
Romão, Maria J.
Trincão, José
author_role author
author2 Kladova, Anna V.
Bursakov, Sergey A.
Dias, João M.
Texeira, Susana
Shnyrov, Valery L.
Moura, José J. G.
Moura, Isabel
Romão, Maria J.
Trincão, José
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Gavel, Olga Yu
Kladova, Anna V.
Bursakov, Sergey A.
Dias, João M.
Texeira, Susana
Shnyrov, Valery L.
Moura, José J. G.
Moura, Isabel
Romão, Maria J.
Trincão, José
dc.subject.por.fl_str_mv ATP sulfurylases
Cobalt
Sulfate-reducing bacteria
Zinc
Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
topic ATP sulfurylases
Cobalt
Sulfate-reducing bacteria
Zinc
Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
description Native zinc/cobalt-containing ATP sulfurylase (ATPS; EC 2.7.7.4; MgATP:sulfate adenylyltransferase) from Desulfovibrio desulfuricans ATCC 27774 was purified to homogeneity and crystallized. The orthorhombic crystals diffracted to beyond 2.5 Å resolution and the X-ray data collected should allow the determination of the structure of the zinc-bound form of this ATPS. Although previous biochemical studies of this protein indicated the presence of a homotrimer in solution, a dimer was found in the asymmetric unit. Elucidation of this structure will permit a better understanding of the role of the metal in the activity and stability of this family of enzymes.
publishDate 2008
dc.date.none.fl_str_mv 2008-01-01
2008-01-01T00:00:00Z
2019-03-11T23:15:26Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1107/S1744309108008816
url https://doi.org/10.1107/S1744309108008816
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1744-3091
PURE: 12013158
http://www.scopus.com/inward/record.url?scp=46949100709&partnerID=8YFLogxK
https://doi.org/10.1107/S1744309108008816
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 3
application/pdf
dc.source.none.fl_str_mv reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron:RCAAP
instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
institution RCAAP
reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
_version_ 1833596467847102464

Similar Items