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Structural Studies of Two Enzymes in the Raetz Pathway of Lipid A Aynthesis, LpxB and LpxH

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자료유형E-Book
개인저자Bohl, Thomas E.
단체저자명University of Minnesota. Biochemistry, Molecular Biology, and Biophysics.
서명/저자사항Structural Studies of Two Enzymes in the Raetz Pathway of Lipid A Aynthesis, LpxB and LpxH.
발행사항[S.l.] : University of Minnesota., 2018
발행사항Ann Arbor : ProQuest Dissertations & Theses, 2018
형태사항178 p.
소장본 주기School code: 0130.
ISBN9780438169364
일반주기 Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
Adviser: Hideki Aihara.
요약Gram-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
요약Lipid 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
요약LpxH 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
요약In 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
일반주제명Biophysics.
Biochemistry.
Microbiology.
언어영어
기본자료 저록Dissertation Abstracts International79-12B(E).
Dissertation Abstract International
대출바로가기http://www.riss.kr/pdu/ddodLink.do?id=T14998845

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