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Structural Studies on SAV0324 from Staphylococcus aureus by X-ray Crystallography
X-선 결정학에 의한 황색포도상구균 유래 SAV0324 단백질의 구조 연구

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Authors
구지성
Advisor
이봉진
Major
약학대학 약학과
Issue Date
2017-08
Publisher
서울대학교 대학원
Keywords
Structure Based Drug Design (SBDD)Staphylococcus aureusX-ray crystallographySAV0324lipoylationvirulence
Description
학위논문 (석사)-- 서울대학교 대학원 약학대학 약학과, 2017. 8. 이봉진.
Abstract
Staphylococcus aureus is a gram positive bacteria which
produces enzymes, toxins, and small RNAs that are often harmful to
the body. About 20-30% of the human population are carriers of the
bacteria and the bacteria is responsible for causing many diseases
and casualties worldwide.
SAV0324 is a glycine cleavage system H-like protein
(GcvH-L) which acts as a carrier for lipoyl moiety. SAV0324
undergoes lipoylation by SAV0327 protein and subsequently undergoes
ADP-ribosylation process. Without ADP-ribosylation, the virulence of
Staphylococcus aureus bacteria decreases and therefore, inhibition of
lipoylation would be crucial.
Using Structure Based Drug Design (SBDD) as a background
knowledge, the structure of SAV0324 protein was determined at
1.88Å. Specifically, SAV0324 conserved five alpha-helices and nine
beta-strands in its structure and the site of lipoylation in SAV0324
was already determined to be E53 (53rd glutamate) and K56 (56th lysine) residues by other researchers. Furthermore, crystallization of
SAV0327 protein was successful. Through binding test between
SAV0324 and SAV0327, the results showed the two proteins did not
have direct binding interaction in the absence of lipoic acid. Thus, in
addition to SAV0324’s structural information, determination of
SAV0327 protein structure and its active site would be of great
significance. Knowing both SAV0324 and SAV0327 thoroughly would
be critical in controlling and understanding bacterial virulence of
Staphylococcus aureus.
Language
English
URI
http://hdl.handle.net/10371/137934
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College of Pharmacy (약학대학)Dept. of Pharmacy (약학과)Theses (Master's Degree_약학과)
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