Backbone NMR assignments of a topologically knotted protein in urea-denatured state
详细信息 查看全文
- 作者：Shu-Ju Micky Hsieh (1)
Anna L. Mallam (2)
Sophie E. Jackson (2)
Shang-Te Danny Hsu (1) (2) (3) (4) - 关键词：Knotted protein ; Protein folding ; Chemical denaturation ; YbeA
- 刊名：Biomolecular NMR Assignments
- 出版年：2014
- 出版时间：October 2014
- 年：2014
- 卷：8
- 期：2
- 页码：283-285
- 全文大小：630 KB
- 参考文献：1. Camilloni C, De Simone A, Vranken WF, Vendruscolo M (2012) Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts. Biochem US 51:2224鈥?231 ternal" href="http://dx.doi.org/10.1021/bi3001825" target="_blank" title="It opens in new window">CrossRef
2. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277鈥?93
3. Hsu ST, Behrens C, Cabrita LD, Dobson CM (2009a) 1H, 15N and 13C assignments of yellow fluorescent protein (YFP) venus. Biomol NMR Assign 3:67鈥?2 ternal" href="http://dx.doi.org/10.1007/s12104-009-9143-y" target="_blank" title="It opens in new window">CrossRef
4. Hsu ST, Cabrita LD, Christodoulou J, Dobson CM (2009b) 1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8聽M urea-denatured states. Biomol NMR Assign 3:29鈥?1 ternal" href="http://dx.doi.org/10.1007/s12104-008-9134-4" target="_blank" title="It opens in new window">CrossRef
5. Mallam AL, Jackson SE (2007) A comparison of the folding of two knotted proteins: YbeA and YibK. J Mol Biol 366:650鈥?65 ternal" href="http://dx.doi.org/10.1016/j.jmb.2006.11.014" target="_blank" title="It opens in new window">CrossRef
6. Mallam AL, Morris ER, Jackson SE (2008a) Exploring knotting mechanisms in protein folding. Proc Natl Acad Sci USA 105:18740鈥?8745 ternal" href="http://dx.doi.org/10.1073/pnas.0806697105" target="_blank" title="It opens in new window">CrossRef
7. Mallam AL, Onuoha SC, Grossmann JG, Jackson SE (2008b) Knotted fusion proteins reveal unexpected possibilities in protein folding. Mol Cell 30:642鈥?48 ternal" href="http://dx.doi.org/10.1016/j.molcel.2008.03.019" target="_blank" title="It opens in new window">CrossRef
8. Mallam AL, Rogers JM, Jackson SE (2010) Experimental detection of knotted conformations in denatured proteins. Proc Natl Acad Sci USA 107:8189鈥?194 ternal" href="http://dx.doi.org/10.1073/pnas.0912161107" target="_blank" title="It opens in new window">CrossRef
9. Purta E, Kaminska KH, Kasprzak JM, Bujnicki JM, Douthwaite S (2008) YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA. RNA 14:2234鈥?244 ternal" href="http://dx.doi.org/10.1261/rna.1198108" target="_blank" title="It opens in new window">CrossRef - 作者单位：Shu-Ju Micky Hsieh (1)
Anna L. Mallam (2)
Sophie E. Jackson (2)
Shang-Te Danny Hsu (1) (2) (3) (4)
1. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
2. Department of Chemistry, University of Cambridge, Cambridge, UK
3. Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan
4. Institue of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan - ISSN：1874-270X
文摘
YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent studies on the knotted protein folding pathways using YbeA have suggested that the protein knot remains present under chemically denaturing conditions. Here, we report 1H, 13C and 15N chemical shift assignments for urea-denatured YbeA, which will serve as the basis for further structural characterisations using solution state NMR spectroscopy with paramagnetic spin labeled and partial alignment media.