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Structural Studies of Two Enzymes in the Raetz Pathway of Lipid A Aynthesis, LpxB and LpxH
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| 자료유형 | E-Book |
|---|---|
| 개인저자 | Bohl, Thomas E. |
| 단체저자명 | University of Minnesota. Biochemistry, Molecular Biology, and Biophysics. |
| 서명/저자사항 | Structural Studies of Two Enzymes in the Raetz Pathway of Lipid A Aynthesis, LpxB and LpxH. |
| 발행사항 | [S.l.] : University of Minnesota., 2018 |
| 발행사항 | Ann Arbor : ProQuest Dissertations & Theses, 2018 |
| 형태사항 | 178 p. |
| 소장본 주기 | School code: 0130. |
| ISBN | 9780438169364 |
| 일반주기 |
Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
Adviser: Hideki Aihara. |
| 요약 | Gram-negative bacteria are distinguished from Gram-positive bacteria by the secondary membrane that surrounds their peptidoglycan cell wall. The outer leaflet of this membrane is primarily composed of the glycolipid lipopolysaccharide (LPS), whi |
| 요약 | Lipid A is synthesized in the well characterized and largely conserved Raetz pathway in the cytosol and at the cytosolic face of the inner membrane. The non-repeating core oligosaccharide is synthesized on lipid A the cytoplasmic face of the inn |
| 요약 | LpxH was crystallized with the alpha-helical substrate-binding cap domain in a displaced conformation, suggesting that this domain is highly mobile. The structural dynamics of this domain and their relevance to substrate binding were further exp |
| 요약 | In addition, the first structure of LpxB was determined showing a Glycosyltransferase B superfamily (GT-B) fold modified by the formation of a novel C-terminally swapped dimer wherein the last 87 residues of one subunit complete the GT-B fold of |
| 일반주제명 | Biophysics. Biochemistry. Microbiology. |
| 언어 | 영어 |
| 기본자료 저록 | Dissertation Abstracts International79-12B(E). Dissertation Abstract International |
| 대출바로가기 | http://www.riss.kr/pdu/ddodLink.do?id=T14998845 |
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| No. | 등록번호 | 청구기호 | 소장처 | 도서상태 | 반납예정일 | 예약 | 서비스 | 매체정보 |
|---|---|---|---|---|---|---|---|---|
| 1 | WE00026294 | 574.191 | 가야대학교// | 대출가능 |
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