Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F02%3A00007110" target="_blank" >RIV/00216224:14310/02:00007110 - 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

Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome

Popis výsledku v původním jazyce

Mycobacterium tuberculosis is a pathogen that is resistant to most common antibiotics and chemotherapeutic agents. This resistance is related to an unusual and well-organized structure of the mycobacterial cell wall that shows an abnormally low degree ofthe hydrophilic permeability. Outer cell wall contains the biochemically unique structures of sugar residues, constituents of various branched and complex polysaccharides and glycolipids . There is very little knowledge about the biosynthesis pathways of these glycoconjugates and about the enzymes, especially glycosyltransferases (GT), involved. The genome of M. tuberculosis contains 3,951 protein-coding sequences. Putative function annotation of some of them was predicted using a combination of sequence alignment and motif comparison . Using this approach, only a small number of putative GTs was identified. Recent crystal structure determination of GTs demonstrated that they adopt only a limited number of topology . We focused on 3D-t

Název v anglickém jazyce

Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome

Popis výsledku anglicky

Mycobacterium tuberculosis is a pathogen that is resistant to most common antibiotics and chemotherapeutic agents. This resistance is related to an unusual and well-organized structure of the mycobacterial cell wall that shows an abnormally low degree ofthe hydrophilic permeability. Outer cell wall contains the biochemically unique structures of sugar residues, constituents of various branched and complex polysaccharides and glycolipids . There is very little knowledge about the biosynthesis pathways of these glycoconjugates and about the enzymes, especially glycosyltransferases (GT), involved. The genome of M. tuberculosis contains 3,951 protein-coding sequences. Putative function annotation of some of them was predicted using a combination of sequence alignment and motif comparison . Using this approach, only a small number of putative GTs was identified. Recent crystal structure determination of GTs demonstrated that they adopt only a limited number of topology . We focused on 3D-t

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2002

Kód důvěrnosti údajů

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

Název statě ve sborníku

XIXčmes Journées de Chimie et Biochimie des Glucides

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

65

Název nakladatele

Societe francaise de Chimie

Místo vydání

France

Místo konání akce

May 20 - 24, Albe, France

Datum konání akce

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Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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