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Molecular recognition and catalysis

Marcus Hartmann

Marcus Hartmann

  • PhD at the MPI for Developmental Biology, 2006-2012
  • Head of the crystallography facility at the MPI since 2009
  • Project leader at the MPI since 2012

Research Interest

The function of biomolecules critically depends on specific interactions with other molecules. Therefore, molecular recognition is pivotal in biomolecular evolution and governs all biochemical processes, from ligand-binding to the assembly of macromolecular complexes.

We study biomolecular interactions in different contexts, employing classical biochemistry, X-ray crystallography, and spectroscopic approaches. On one end, we are interested in substrate recognition and biocatalysis. We probe the substrate spectrum and dissect the molecular mechanism of enzymes, with a focus on proteins of yet unknown function and on potential drug targets. On the other end, we are investigating regulatory protein-protein interactions in two different lines of research. In one, we are using natural bifunctional fusion enzymes to investigate how the individual proteins of metabolic pathways are potentially organized for efficient substrate funneling or feedback regulation via allosteric effects. In the other, we aim to probe the druggability of protein-protein interfaces in macromolecular complexes implicated in human disease.

Selected Reading

1) Hartmann MD, Boichenko I, Coles M, Zanini F, Lupas AN, Hernandez Alvarez B. (2014) Thalidomide mimics uridine binding to an aromatic cage in cereblon. J Struct Biol 188, 225-32.

2) Chellamuthu VR, Ermilova E, Lapina T, Lüddecke J, Minaeva E, Herrmann C, Hartmann MD, Forchhammer K. (2014) A widespread glutamine-sensing mechanism in the plant kingdom. Cell 159, 1188-99.

3) Mir-Montazeri B, Ammelburg M, Forouzan D, Lupas AN, Hartmann MD. (2011) Crystal structure of a dimeric archaeal cleavage and polyadenylation specificity factor. J Struct Biol 173, 191-5.
(click to enlarge) Crystallographic snapshots of the cereblon thalidomide binding domain, as it gradually unfolds upon release of its ligand