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020 ▼a 9780438169364
035 ▼a (MiAaPQ)AAI10826099
035 ▼a (MiAaPQ)umn:19283
040 ▼a MiAaPQ ▼c MiAaPQ ▼d 248032
0820 ▼a 574.191
1001 ▼a Bohl, Thomas E.
24510 ▼a Structural Studies of Two Enzymes in the Raetz Pathway of Lipid A Aynthesis, LpxB and LpxH.
260 ▼a [S.l.] : ▼b University of Minnesota., ▼c 2018
260 1 ▼a Ann Arbor : ▼b ProQuest Dissertations & Theses, ▼c 2018
300 ▼a 178 p.
500 ▼a Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
500 ▼a Adviser: Hideki Aihara.
5021 ▼a Thesis (Ph.D.)--University of Minnesota, 2018.
520 ▼a 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
520 ▼a 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
520 ▼a 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
520 ▼a 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
590 ▼a School code: 0130.
650 4 ▼a Biophysics.
650 4 ▼a Biochemistry.
650 4 ▼a Microbiology.
690 ▼a 0786
690 ▼a 0487
690 ▼a 0410
71020 ▼a University of Minnesota. ▼b Biochemistry, Molecular Biology, and Biophysics.
7730 ▼t Dissertation Abstracts International ▼g 79-12B(E).
773 ▼t Dissertation Abstract International
790 ▼a 0130
791 ▼a Ph.D.
792 ▼a 2018
793 ▼a English
85640 ▼u http://www.riss.kr/pdu/ddodLink.do?id=T14998845 ▼n KERIS
980 ▼a 201812 ▼f 2019
990 ▼a 관리자