Solution Structure of Slc11a2-TM6 in Dodecylphosphocholine Micelles†

doi:10.7503/cjcu20160884

Abstract

Abstract:

The structure of isolated peptides from TM6 of Slc11a2 in dodecylphosphocholine(DPC) micelles was investigated using circular dichroism(CD) and nuclear magnetic resonance(NMR) spectroscopy. The results reveal that TM6 of Slc11a2 forms short α-helix in both N- and C-terminal and the two α-helixes are connected by a highly flexible region, the whole peptide is embedded in DPC micelles. H267A mutation makes the helix become longer, while H272A mutation make the helix become slightly shorter.

Key words: Slc11a2-TM6, Nuclear magnetic resonance, 3D structure(Ed.: S, Z, M)

CLC Number:

O629.7

TrendMD:

XIAO Shuyan, LI Fei, DONG Zhongping. Solution Structure of Slc11a2-TM6 in Dodecylphosphocholine Micelles^†[J]. Chem. J. Chinese Universities, 2017, 38(9): 1596.

Figures/Tables 5

Fig.1 CD spectra of Slc11a2-TM6(a), H267A(b) and H272A(c) in DPC micelles at pH=4.12 and room temperature

Fig.2 Hα-HN region of 2D NOESY spectra of Slc11a2-TM6 in 90%H2O/10%D2O, 298 K(A), Hα-HN region of 2D NOESY spectra(B), the NOE connectivities(C) and secondary structure shift(D) of Slc11a2-TM6 in the presence of 240 mmol/L DPC-d38 at pH=4.12 and 298 K

Fig.3 Ensemble of backbone atoms of 10 best structures(A) and ribbon representation of the mean

Table 1 Structural statistics of Slc11a2-TM6 in DPC-d38 micelles at pH=4.12 and 298 K

Deviations from idealized geometry	Bond lengths/nm	0.0005
	Bond angles/(°)	0.4
RMSD values(All residues)	Backbone heavy atoms/nm	0.21
	All heavy atoms/nm	0.28
RMSD values(well-defined residues^*)	Backbone heavy atoms/nm	0.01
	All heavy atoms/nm	0.06
Ramachandran plot statistics(well-defined residues^*)	Residues in most favored region(%)	100.0
	Residues in additionally allowed region(%)	0
	Residues in generously allowed region(%)	0
	Residues in disallowed region(%)	0

Fig.4 Effects of Mn2+ ions on the resonance intensities of Slc11a2-TM6 in DPC-d38 micelles at 298 K

References 33

[1]	Aizenman E., Mastroberardino P. G., Neurobiol. Dis., 2015, 81, 1—3
[2]	White A. R., Kanninen K. M., Crouch P. J., Front. Aging. Neurosci., 2015, 7, 127
[3]	Mackenzie B., Hediger M. A., Pflugers Arch., 2004, 447(5), 571—579
[4]	Gruenheid S., Cellier M., Vidal S., Gros P., Genomics,1995, 25(2), 514—525
[5]	Agranoff D., Monahan I. M., Mangan J. A., Butcher P. D., Krishna S., J. Exp. Med., 1999, 190(5), 717—724
[6]	D Souza J., Cheah P. Y., Gros P., Chia W., Rodrigues V., J. Exp. Biol., 1999, 202(14), 1909—1915
[7]	Dorschner M. O., Phillips R. B., DNA Cell Biol., 1999, 18(7), 573—583
[8]	Zoller H., Pietrangelo A., Vogel W., Weiss G., Lancet,1999, 353(9170), 2120—2123
[9]	Fleming R. E., Migas M. C., Zhou X., Jiang J., Britton R. S., Brunt E. M., Tomatsu S., Waheed A., Bacon B. R., Sly W. S., Proc. Natl. Acad. Sci. USA,1999, 96(6), 3143—3148
[10]	Xue X., Ramakrishnan S. K., Weisz K., Triner D., Xie L., Attili D., Pant A., Gyorffy B., Zhan M., Carter-Su C., Hardiman K. M., Wang T. D., Dame M. K., Varani J., Brenner D., Fearon E. R., Shah Y. M., Cell Metab., 2016, 24(3), 447—461
[11]	Mackenzie B., Ujwal M. L., Chang M. H., Romero M. F., Hediger M. A., Pflugers Arch., 2006, 451(4), 544—558
[12]	Lam-Yuk-Tseung S., Govoni G., Forbes J., Gros P., Blood,2003, 101(9), 3699—3707
[13]	Arora A., Tamm L. K., Curr. Opin. Struct. Biol., 2001, 11(5), 540—547
[14]	Qi H. Y., Tang W. X., Bai L. M., Guo L. D., Chem. Res. Chinese Universities, 2017, 33(2), 221—226
[15]	Seddon A. M., Curnow P., Booth P. J., Biochim. Biophys. Acta, 2004, 1666(1/2), 105—117
[16]	Wang S., Yu J. Y., Li W., Li F., Chem. J. Chinese Universities, 2011, 32(4), 915—919
	(王硕, 于佳一, 李惟, 李菲.高等学校化学学报,2011, 32(4), 915—919)
[17]	Nie X. H., Zhang T., Li Y., Zheng X. F., Cao H. Y., Tang Q., Chem. J. Chinese Universities, 2010, 31(7), 1337—1341
	(聂新华, 张涛, 李元, 郑学仿, 曹洪玉, 唐乾.高等学校化学学报,2010, 31(7), 1337—1341)
[18]	Xiao S. Y., Wang C. Y., Li J. T., Li F., J. Pept. Sci., 2011, 17(7), 505—511
[19]	Xiao S. Y., Li J. T., Wang Y. X., Wang C. Y., Xue R., Wang S., Li F., Biochim. Biophys. Acta, 2010, 1798(8), 1556—1564
[20]	Sreerama N., Woody R. W., Anal. Biochem., 2000, 287(2), 252—260
[21]	Goddard T.D., Kneller D. G., Sparky3, University of California,San Francisco, 2001
[22]	Lange O. F., Rossi P., Sgourakis N. G., Song Y., Lee H. W., Aramini J. M., Ertekin A., Xiao R., Acton T. B., Montelione G. T., Baker D., Proc. Natl. Acad. Sci. USA,2012, 109(27), 10873—10878
[23]	Zhang Y. H., Li L. C., Yuan W. C., Zhang X. M., Chem. Res. Chinese Universities, 2015, 31(3), 381—387
[24]	Yang L., Li J. T., Qi H.Y., Li. F., Chem. Res. Chinese Universities, 2012, 28(4), 732—736
[25]	Greenfield N. J., Anal. Biochem., 1996, 235(1), 1—10
[26]	Seddon A. M., Curnow P., Booth P. J., Biochim. Biophys. Acta, 2004, 1666, 105—117
[27]	Wishart D. S., Sykes B. D., Richards F. M., J. Mol. Biol., 1991, 222(2), 311—333
[28]	Manzo G., Casu M., Rinaldi A. C., Montaldo N. P., Luganini A., Gribaudo G., Scorciapino M. A., J. Nat. Prod., 2014, 77(11), 2410—2417
[29]	Courville P., Urbankova E., Rensing C., Chaloupka R., Quick M., Cellier M. F., J. Biol. Chem., 2008, 283(15), 9651—9658
[30]	Screpanti E., Hunte C., J. Struct. Biol., 2007, 159(2), 261—267
[31]	Arkin I. T., Xu H., Jensen M. O., Arbely E., Bennett E. R., Bowers K. J., Chow E., Dror R. O., Eastwood M. P., Flitman-Tene R., Gregersen B. A., Klepeis J. L., Kolossvary I., Shan Y., Shaw D. E., Science,2007, 317(5839), 799—803
[32]	Hunte C., Screpanti E., Venturi M., Rimon A., Padan E., Michel H., Nature,2005, 435(7046), 1197—1202
[33]	Toyoshima C., Nakasako M., Nomura H., Ogawa H., Nature,2000, 405(6787), 647—655