Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine beta-Synthase: Study by Differential Covalent Labeling and Computational Modeling

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F10%3A7639" target="_blank" >RIV/00216208:11110/10:7639 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/10:00024202 RIV/00064165:_____/10:7639

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine beta-Synthase: Study by Differential Covalent Labeling and Computational Modeling

Popis výsledku v původním jazyce

Cystathionine ?-synthase (CBS) is a modular enzyme which catalyzes condensation of serine with homocysteine. The atomic mechanisms of the CBS allostery have not yet been sufficiently explained. To determine the contact area between the catalytic core andthe autoinhibitory module of the CBS protein, we compared side-chain reactivity of the truncated CBS lacking the regulatory domain (45CBS) and of the full-length enzyme (wtCBS) using covalent labeling by six different modification agents and subsequentmass spectrometry. Fifty modification sites were identified in 45CBS, and four of them were not labeled in wtCBS. One differentially reactive site (cluster W408/W409/W410) is a part of the linker between the domains. The other three residues (K172 and/orK177, R336, and K384) are located in the same region of the 45CBS crystal structure; computational modeling showed that these amino acid side chains potentially form a regulatory interface in CBS protein.

Název v anglickém jazyce

Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine beta-Synthase: Study by Differential Covalent Labeling and Computational Modeling

Popis výsledku anglicky

Cystathionine ?-synthase (CBS) is a modular enzyme which catalyzes condensation of serine with homocysteine. The atomic mechanisms of the CBS allostery have not yet been sufficiently explained. To determine the contact area between the catalytic core andthe autoinhibitory module of the CBS protein, we compared side-chain reactivity of the truncated CBS lacking the regulatory domain (45CBS) and of the full-length enzyme (wtCBS) using covalent labeling by six different modification agents and subsequentmass spectrometry. Fifty modification sites were identified in 45CBS, and four of them were not labeled in wtCBS. One differentially reactive site (cluster W408/W409/W410) is a part of the linker between the domains. The other three residues (K172 and/orK177, R336, and K384) are located in the same region of the 45CBS crystal structure; computational modeling showed that these amino acid side chains potentially form a regulatory interface in CBS protein.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Biochemistry

ISSN

0006-2960

e-ISSN

—

Svazek periodika

49

Číslo periodika v rámci svazku

49

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

—

Kód UT WoS článku

000284975000018

EID výsledku v databázi Scopus

—