Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
| Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus | |
| Wang, Tao1; Langer, Julian D.1; Peng, Guohong1,2; Michel, Hartmut1; Peng, GH (reprint author), Max Planck Inst Biophys, Dept Mol Membrane Biol, Max von Laue Str 3, D-60438 Frankfurt, Germany. | |
| 2012-12-01 | |
| Source Publication | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| ISSN | 1570-9639 |
| Volume | 1824Issue:12Pages:1358-1365 |
| Subtype | Article |
| Abstract | The "hypothetical protein" Aq_1259 was identified by mass spectrometry and purified from native membranes of Aquifex aeolicus. It is a 49.4 kDa protein, highly homologous (>52% identity) to several conserved hypothetical proteins from other bacteria. However, none of these proteins has been characterized using biochemical or electrophysiological techniques. Based on the sequence and circular dichroism spectroscopy, the structure of Aq_1259 is predicted to be a beta-barrel with 16 beta-strands. The strands with loops and turns are distributed evenly through the entire sequence. The function of Aq_1259 was analyzed after incorporation into a lipid bilayer. Electrophysiological measurements revealed a pore that has a basic stationary conductance of 0.48 +/- 0.038 nS in a buffer with 0.5 M NaH2PO4 at pH 6.5 and 0.2 +/- 0.015 nS in a buffer with 0.5 M NaCl at pH 6.5. Superimposed on this is a fluctuating conductance of similar amplitude. Aq_1259 could be crystallized. The crystals diffract to a resolution of 3.4 angstrom and belong to space group 1222 with cell dimensions of a = 138.3 angstrom, b = 144.6 angstrom, c = 151.8 angstrom. (C) 2012 Elsevier B.V. All rights reserved. |
| Keyword | Aq_1259 Porin Aquifex Aeolicus Hypothetical Protein |
| Subject Area | Biochemistry & Molecular Biology ; Biophysics |
| DOI | 10.1016/j.bbapap.2012.07.004 |
| URL | 查看原文 |
| Indexed By | SCI |
| Language | 英语 |
| WOS ID | WOS:000310761700006 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.qdio.ac.cn/handle/337002/12356 |
| Collection | 实验海洋生物学重点实验室 |
| Corresponding Author | Peng, GH (reprint author), Max Planck Inst Biophys, Dept Mol Membrane Biol, Max von Laue Str 3, D-60438 Frankfurt, Germany. |
| Affiliation | 1.Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany 2.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China |
| Recommended Citation GB/T 7714 | Wang, Tao,Langer, Julian D.,Peng, Guohong,et al. Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2012,1824(12):1358-1365. |
| APA | Wang, Tao,Langer, Julian D.,Peng, Guohong,Michel, Hartmut,&Peng, GH .(2012).Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1824(12),1358-1365. |
| MLA | Wang, Tao,et al."Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1824.12(2012):1358-1365. |
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