Reaction Mechanism of MutH Enzyme - Quantum Mechanics/Molecular Mechanics Study 2

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F11%3A00050263" target="_blank" >RIV/00216224:14310/11:00050263 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Reaction Mechanism of MutH Enzyme - Quantum Mechanics/Molecular Mechanics Study 2

Popis výsledku v původním jazyce

Knowledge of enzymes reaction mechanisms can be helpful in many fields such as biology, medicine or pharmacy. In our study, we are focused on MutH enzyme, which is an integral part of Methyl-directed Mismatch Repair together with MutL and MutS enzymes. Amismatch introduced during DNA replication is recognized by MutS enzyme, information about the mismatch is transferred through MutL to MutH enzyme. MutH specifically recognizes the GATC sequence on daughter DNA strand and cleaves this strand close to the G base. Wrong paired base is removed and after that the correct base pairing is reestablished [1]. Main goal of our project is the understanding of the reaction mechanism of MutH enzyme. We present the Quantum Mechanics / Molecular Mechanics (QM/MM) study of the MutH enzyme reactivity based on models prepared from the available crystal structures of protein / DNA complex [2]. The cleavage mechanism is studied on ab-initio level using CPMD implementation of Density Functional Theory.

Název v anglickém jazyce

Reaction Mechanism of MutH Enzyme - Quantum Mechanics/Molecular Mechanics Study 2

Popis výsledku anglicky

Knowledge of enzymes reaction mechanisms can be helpful in many fields such as biology, medicine or pharmacy. In our study, we are focused on MutH enzyme, which is an integral part of Methyl-directed Mismatch Repair together with MutL and MutS enzymes. Amismatch introduced during DNA replication is recognized by MutS enzyme, information about the mismatch is transferred through MutL to MutH enzyme. MutH specifically recognizes the GATC sequence on daughter DNA strand and cleaves this strand close to the G base. Wrong paired base is removed and after that the correct base pairing is reestablished [1]. Main goal of our project is the understanding of the reaction mechanism of MutH enzyme. We present the Quantum Mechanics / Molecular Mechanics (QM/MM) study of the MutH enzyme reactivity based on models prepared from the available crystal structures of protein / DNA complex [2]. The cleavage mechanism is studied on ab-initio level using CPMD implementation of Density Functional Theory.

Druh

O - Ostatní výsledky

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů