메뉴 건너뛰기




Volumn 331, Issue 6017, 2011, Pages 589-592

Directed evolution of a protein container

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; PROTEIN;

EID: 79551616431     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1199081     Document Type: Article
Times cited : (268)

References (35)
  • 6
    • 34247383568 scopus 로고    scopus 로고
    • S. Jenni et al., Science 316, 254 (2007).
    • (2007) Science , vol.316 , pp. 254
    • Jenni, S.1
  • 17
    • 0028887435 scopus 로고
    • T. Douglas et al., Science 269, 54 (1995).
    • (1995) Science , vol.269 , pp. 54
    • Douglas, T.1
  • 19
    • 0142043370 scopus 로고    scopus 로고
    • M. Knez et al., Nano Lett. 3, 1079 (2003).
    • (2003) Nano Lett. , vol.3 , pp. 1079
    • Knez, M.1
  • 20
    • 0037497251 scopus 로고    scopus 로고
    • D. Ishii et al., Nature 423, 628 (2003).
    • (2003) Nature , vol.423 , pp. 628
    • Ishii, D.1
  • 23
  • 24
    • 2142803437 scopus 로고    scopus 로고
    • Materials and methods are available as supporting material on
    • Materials and methods are available as supporting material on Science Online.
    • Science Online
  • 29
    • 79551623928 scopus 로고    scopus 로고
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
  • 32
    • 79551616480 scopus 로고    scopus 로고
    • note
    • Wild-type lumazine synthases adopt multiple assembly forms depending on the choice of buffer and pH. Thus, in addition to T = 1 and T = 3 capsids with diameters around 16 and 30 nm, respectively, a larger structure consistent with either an expanded T = 3 or a T = 4 state has been observed by small angle x-ray scattering experiments (26). Under the conditions used in the current study, AaLS-neg assembles predominantly as conventional T = 3 capsids, whereas the evolved variant appears to favor the larger expanded form, both in the presence and absence of HIV protease. Although the observed shift in population can be ascribed to the increase in net negative charge on each monomer, detailed structural experiments will be needed to resolve whether it reflects a subtle subunit rearrangement or an increase in T number.
  • 35
    • 79551632398 scopus 로고    scopus 로고
    • note
    • We thank B. Roschitzki at the Functional Genomics Center Zürich for collection of mass spectrometic data and assistance with data analysis; T. Ishikawa and M. Lucas at the Electron Microscopy Center of the ETH Zürich (EMEZ) for collecting the EM images and assistance with EM data analysis; H.-M. Fischer, F. Narberhaus, M. Neuenschwander, and F. Seebeck for contributive discussions; and P. Kast for careful reading of the manuscript. This work was supported in part by the Schweizerischer Nationalfond and the ETH Zürich. The supercharged GFP described in fig. S8 was obtained under a materials transfer agreement (MTA) with D. R. Liu at Harvard. An MTA would be required for sharing of materials used in the reported research.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.