Patrícia Castellen

Brazilian Biosciences National Laboratory

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Sérgio Ricardo de Lázaro

Universidade Estadual de Ponta Grossa

Karen Wohnrath

Universidade Estadual de Ponta Grossa

Ivelise Dimbarre Lao Guimarães

Universidade Estadual de Ponta Grossa

Renè T. Boeré

University of Lethbridge

Flávia Marszaukowski

Universidade Estadual de Ponta Grossa

Renan Augusto Pontes Ribeiro

Universidade do Estado de Minas Gerais

Ellen Wrobel

Universidade de São Paulo

Frederico J. Gueiros‐Filho

Universidade de São Paulo

Ana Carolina de Mattos Zeri

Brazilian Biosciences National Laboratory

Maurício L. Sforça

Brazilian Center for Research in Energy and Materials

Cooperative Institutions

Universidade de São Paulo

Universidade Estadual de Ponta Grossa

Universidade Estadual de Campinas (UNICAMP)

Universidade Federal do Paraná

Universidade Federal de São Carlos

Brazilian Center for Research in Energy and Materials

Centro de Investigaciones Biológicas Margarita Salas

Brazilian Biosciences National Laboratory

Universidade Estadual Paulista (Unesp)

Consejo Superior de Investigaciones Científicas

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Análise estrutural e funcional da regiăo gInBA de Azospirillum brasilense

Patrícia Castellen

Azospirillum brasilense

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Citations (1)

Structural organization of the glnBA region of the Azospirillum brasilense genome

European Journal of Soil Biology (2008)

Patrícia Castellen Roseli Wassem Rose A. Monteiro Leonardo M. Cruz Maria Berenice Reynaud Steffens

Azospirillum brasilense

Structural gene

10.1016/j.ejsobi.2008.09.010

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Citations (6)

CCDC 1894829: Experimental Crystal Structure Determination

The Cambridge Structural Database (2022)

Ivelise Dimbarre Lao Guimarães Flávia Marszaukowski Priscila Buhrer Rutka Luis Felipe Borge Renan Augusto Pontes Ribeiro

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

10.5517/ccdc.csd.cc21lqjx

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The Streptococcus mutans GlnR protein exhibits an increased affinity for the glnRA operon promoter when bound to GlnK

DOAJ (DOAJ: Directory of Open Access Journals) (2011)

Patrícia Castellen Fabiane Gomes de Moraes Rego Magda Eline Guerrart Portugal Elaine Machado Benelli

gal operon

10.1590/s0100-879x2011001200002

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Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis

Biomolecular NMR Assignments (2013)

Patrícia Castellen Maurício L. Sforça Frederico J. Gueiros‐Filho Ana Carolina de Mattos Zeri

FtsZ

10.1007/s12104-013-9534-y

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NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex.

bioRxiv (Cold Spring Harbor Laboratory) (2024)

Luciana E. S. F. Machado Patrícia Castellen Valdir Blasios Helder Veras Ribeiro Filho Alexandre W. Bisson‐Filho

Abstract The Min system is a key spatial regulator of cell division in rod-shaped bacteria and the first FtsZ negative modulator to be recognized. Nevertheless, despite extensive genetic and in vitro studies, the molecular mechanism used by MinC to inhibit Z-ring formation remains incompletely understood. The crystallization of FtsZ in complex with other negative regulators such as SulA and MciZ has provided important structural information to corroborate in vitro experiments and establish the mechanism of Z-ring antagonism by these modulators. However, MinC and FtsZ have so far eluded co-crystallization, probably because their complex is too unstable to be crystallized. To gain structural insight into the mechanism of action of MinC, we determined the solution structure of the N-terminal domain of B. subtilis MinC, and through NMR titration experiments and mutagenesis identified the binding interfaces involved in the MinC N -FtsZ interaction. By using our experimental results as restraints in docking, we also constructed a molecular model for the FtsZ:MinC N complex and validated it by molecular dynamics. The model shows that MinC N binding overlaps with the FtsZ polymerization interface on the C-terminal globular subdomain of FtsZ and, thus, provides a structural basis for MinC N inhibition of FtsZ filament formation. Given that the C-terminal polymerization interface of FtsZ corresponds to the plus end of FtsZ filaments, we propose that capping is the main mechanism employed by MinC to antagonize FtsZ polymerization.

FtsZ

10.1101/2024.03.31.587266

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Citations (0)

CCDC 1891875: Experimental Crystal Structure Determination

The Cambridge Structural Database (2020)

Ivelise Dimbarre Lao Guimarães Flávia Marszaukowski Renan Augusto Pontes Ribeiro Sérgio Ricardo de Lázaro Katia M. Oliveira

10.5517/ccdc.csd.cc21hn7g

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CCDC 2163114: Experimental Crystal Structure Determination

The Cambridge Structural Database (2022)

Ivelise Dimbarre Lao Guimarães Flávia Marszaukowski Priscila Buhrer Rutka Luis Felipe Borge Renan Augusto Pontes Ribeiro

10.5517/ccdc.csd.cc2blwwq

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FtsZ filament capping by MciZ, a developmental regulator of bacterial division

Proceedings of the National Academy of Sciences (2015)

Alexandre W. Bisson‐Filho Karen Fulan Discola Patrícia Castellen Valdir Blasios Alexandre Martins

Significance Division of bacteria is executed by a contractile ring whose cytoskeletal framework is FtsZ (filamentation temperature-sensitive Z), a protein evolutionarily related to eukaryotic tubulin. The FtsZ ring is made of filaments of head-to-tail FtsZ subunits but its architecture and the rules governing its assembly are still poorly known. Here we show that MciZ, an inhibitor of FtsZ ring formation, functions by capping the minus end of FtsZ filaments. Capping by MciZ makes FtsZ filaments shorter than normal, likely by blocking filament annealing; this represents fundamental information to understand how FtsZ filaments grow and shrink, and attain their normal size. The powerful inhibition of Z-ring assembly by MciZ also suggests that an FtsZ ring cannot form from filaments smaller than a certain size.

FtsZ

Filamentation

10.1073/pnas.1414242112

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Citations (69)

CCDC 1891881: Experimental Crystal Structure Determination

The Cambridge Structural Database (2020)

Ivelise Dimbarre Lao Guimarães Flávia Marszaukowski Renan Augusto Pontes Ribeiro Sérgio Ricardo de Lázaro Katia M. Oliveira

10.5517/ccdc.csd.cc21hnfn

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