Gunter Schneider group

Research at the division is supported by Karolinska Institutet, the Swedish Science Council (VR), and VINNOVA.

Research projects

Structural enzymology of the biosynthesis of polyketide antibiotics

Anthracyclines are secondary metabolites of Streptomyces, and members of this class of polyketide antibiotics belong to the most-used chemotherapeutic agents in the combat against cancer. The research program aims at the elucidation of the structural enzymology of anthracycline biosynthesis. Target selection is focused on enzymes not related in sequence to proteins of known structure, and/or novel enzymatic mechanisms.

The project is lead by Gunter Schneider.

Structural biology of bacterial pathogens

This research project aims at the structural and functional characterization of proteins and protein complexes from major pathogens, in particular Gram–negative bacteria and Mycobacterium tuberculosis. One of the objectives of this program is to provide sufficient structural and mechanistic insights to facilitate the design of strong binding inhibitors, which may be developed into novel drugs.

The project is lead by Gunter Schneider and Robert Schnell.

Development of soft- and hardware for macromolecular crystallography

For more information, see Lohkamp group.

Structures

Here a selection of structures solved in our lab. A complete list is available at the Protein Data Bank.

SnoK/N couple

5EPA, 5EQU, 5ERL, 5EP9

Divergent non-heme iron enzymes in the nogalamycin biosynthetic pathway.
Siitonen V, Selvaraj B, Niiranen L, Lindqvist Y, Schneider G, Metsä-Ketelä M
Proc. Natl. Acad. Sci. U.S.A. 2016 May;113(19):5251-6

Arthritogenic Antibody-collagen complex

4BKL

Epitope-specific antibody response is controlled by immunoglobulin V(H) polymorphisms.
Raposo B, Dobritzsch D, Ge C, Ekman D, Xu B, Lindh I, et al
J. Exp. Med. 2014 Mar;211(3):405-11

SnoaL

1SJW

Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation.
Sultana A, Kallio P, Jansson A, Wang JS, Niemi J, Mäntsälä P, et al
EMBO J. 2004 May;23(9):1911-21

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, et al
Science 1999 Jun;284(5420):1667-70

Ketoacyl ACP-synthase II

1E5M, 1B3N, 1KAS

Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y
EMBO J. 1998 Mar;17(5):1183-91

Nitrile hydratase

1AHJ

Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold.
Huang W, Jia J, Cummings J, Nelson M, Schneider G, Lindqvist Y
Structure 1997 May;5(5):691-9

Desaturase

1AFR, 1OQ4, 1OQ7, 1OQ9, 1OQB, 2J2F, 2UW1

Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins.
Lindqvist Y, Huang W, Schneider G, Shanklin J
EMBO J. 1996 Aug;15(16):4081-92

Transketolase

1GPU, 1AYO , 1NGS, 1TRK, 1TKB, 1TKC, 1TKA, 1R9J

Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.
Lindqvist Y, Schneider G, Ermler U, Sundström M
EMBO J. 1992 Jul;11(7):2373-9

Research group