Data Bank Depositions

Essential proteins from African trypanosomes:

  • dynamics of the redox states of an oxidoreductase from trypanosomes
  • an unexpected inhibitor-induced dimerization of an essential parasitic oxidoreductase


BMRB: 27049, 27050


published in:

Wagner, A., Le, T.A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A.K., Dirdjaja, N., Krauth-Siegel, R.L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angewandte Chemie Int. Ed. accepted Angew. Chem. Int. Ed. 10.1002/anie.201810470

Wagner, A., Diehl, E., Krauth-Siegel, R.L., Hellmich, U. A. (2017) Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form. Biomol. NMR Assign. 11(2):193-196.


TRP ion channels:

  • Structure of the TRPV4 ion channel N-terminus in complex with the PACSIN/Syndapin SH3 domain uncovers a novel binding mode
  • First structure of a TRPML2 ion channel domain allows to deduce a rational basis for pH-dependent cation gating in the endolysosomal compartments.

PDB: 6F55, 6HRR, 6HHRS

BMRB: 34211


published in:

Viet, K.K., Wagner, A., Schickert, K., Hellmwig, N., Brennich, M., Bader, N., Schirmeister, T., Morgner, N., Schindelin, H., Hellmich, U. A. (2019) Structure of the human TRPML2 ion channel extracytosolic/lumenal domain. Structure accepted.

Goretzki, B., Glogowski, N.A., Diehl, E., Duchardt-Ferner, E., Hacker, C., Gaudet, R., Hellmich#, U. A. (2018) Structural basis of TRPV4 N-terminus interaction with Syndapin/PACSIN1-3 and PIP2. Structure, 26(12):1583-1593


(L)antibiotic resistance proteins:

BMRB: 17660, 25175, 25193, 25194,  17534

PDB: 2N2E, 2N32, 2LVL

published in:

Hellmich#, U.A., Mönkemeyer L, Velamakanni S, van Veen HW, Glaubitz C. (2015) Effects of nucleotide binding to LmrA: A combined MAS-NMR and solution NMR study. Biochim. Biophys. Acta Biomembr. 1848(12):3158-65. (#corresponding author)

Hacker, C., Christ, N. A., Duchardt-Ferner,E., Korn, S., Göbl, C., Berninger, L., Düsterhus, S., Hellmich, U. A., Madl, T., Kötter, P., Entian, K., Wöhnert, J. (2015) The solution structure of the lantibiotic immunity protein NisI and its interactions with nisin. J. Biol. Chem. 290(48):28869-86.

Christ, N.A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U.A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.D. and Wöhnert, J. (2012) The first structure of a LanI protein, SpaI: The protein conferring autoimmunity against the lantibiotic subtilin in Bacillus subtilis reveals a novel fold.  J. Biol. Chem. 287(42):35286-98.

Hellmich*, U.A., Lyubenova*, S., Kaltenborn, E., Doshi, R., van Veen, H. W., Prisner, T.F. and Glaubitz, C. (2012) Probing the ATP hydrolysis cycle of the ABC multidrug transporter LmrA by pulsed EPR Spectroscopy. J. Am. Chem. Soc., 134(13):5857-62.(*contributed equally)

Hellmich, U.A., Duchardt-Ferner, E., Glaubitz, C. and Wöhnert, J. (2012) Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state. Biomol. NMR Assign. 6(1):69-73.


Other projects:

BMRB: 18031, 27683


published in:

Heiby*, J., Goretzki*, B., Johnson, C., Hellmich#, U.A., Neuweiler,# H. (2019) currently under review. (*contributed equally, #co-corresponding authors)

Hellmich, U.A., Weis, B.L., Luitikov, A., Wurm, J.P., Christ, N.A., Hantke, K., Kötter, P., Entian, K.D., Schleiff, E. and Wöhnert, J. (2013) Essential ribosome assembly factor Fap7 regulates a hierarchy of RNA-protein interactions during small ribosomal subunit biogenesis. Proc. Nat. Acad. Sci. USA 110(38):15253-8.

Hellmich, U.A. and Wöhnert, J. (2013) Backbone resonance assignments for a homolog of the essential ribosome biogenesis factor Fap7 from P. horikoshii in its nucleotide-free and -bound forms. Biomol. NMR Assign. 7(2):261-5.



We thank the Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-Universität Frankfurt

ESRF, Grenoble (beamlines ID29, ID23-1, BM29)

BESSY II, Helmholtz Zentrum Berlin (beamline 14.1)

for excellent technical suppport