Expression and purification of putative mycobacterial glycosyltransferase Rv3782 for crystallographic studies
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00009308" target="_blank" >RIV/00216224:14310/03:00009308 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Expression and purification of putative mycobacterial glycosyltransferase Rv3782 for crystallographic studies
Original language description
A putative rhamnosyltransferase Rv3782 belongs to a group of glycosyltansferases (GTs) that are responsible for biosynthesis of cell wall envelope of Mycobacterium tuberculosis. Mycobacterial cell wall contains some unique sugar components that play a crucial role in host-pathogen interaction and is responsible for high pathogen resistance against common therapeutic agents. Thus these GTs are interesting as potential drug targets. In previous part of our research we selected some genes of putative GTs (using various bioinformatics tools applied to M. tuberculosis H37Rv genome sequence) that should be mostly of interest. At present study we have been focused on structural analysis of Rv3782. The main problem is to obtain a sufficient amount of soluble and pure protein for crystallization studies. Most of the expressed protein forms inclusion bodies, probably because of its toxicity for host cells, and there are additional losses caused by high GTs hydrofobicity that complicates its puri
Czech name
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Czech description
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Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
VII. pracovní setkání biochemiků a molekulárních biologů
ISBN
80-210-3053-4
ISSN
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e-ISSN
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Number of pages
1
Pages from-to
26
Publisher name
Masarykova univerzita
Place of publication
Brno
Event location
Brno
Event date
Jan 1, 2003
Type of event by nationality
CST - Celostátní akce
UT code for WoS article
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