From left to right: Klaus Pantel (UKE), Stefan Werner (UKE), Nishit Goradia UKE, previously EMBL), Matthias Wilmanns (EMBL, UKE).
@nishitgoradia.bsky.social, previous postdoc at @embl.org, and Stefan Werner from the University Hamburg Clinical Center received this year's Research Award of the Hamburg Cancer Society for their work published in www.nature.com/articles/s41467-024-49488-3. Our congratulations to both of you!
Great to see all these structures posted 😊 Amazing what endogenous extraction and purification can do. Congratulations to John and colleagues!
Cryo-EM maps and atomic models of the biotin-containing 3-methylcrotonyl-CoA carboxylase (MCC) complex and long-chain acyl-CoA carboxylase (LCC) complex
New lab preprint!
@zestytoast.bsky.social tagged a scarce mycobacterial protein in M. smegmatis with TwinStep but got… something? @kjamali.bsky.social's ModelAngelo built models & @martinsteinegger.bsky.social's FoldSeek IDed them as the biotin-containing MCC & LCC complexes
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tinyurl.com/ukny4ptz
Binding of acyl-CoA substrates in AccA3/AccD4/AccD5/AccE5 causes a ~90 deg. rotation of the uneven 9-stranded (AccA3)4/AccE5 beta-barrel. The rotation propagates into the complete AccA3 assembly, which is split into two asymmetric AccA3 dimers.
A C-terminal helical dimerization module in the AccE5 subunit is responsible for the chimeric assembly of two related acyl-CoA carboxyl transferase subunits (AccD4, AccD5). Each of them specifically catalyzes carboxylation of long-chain and short chain acyl-CoAs, respectively.
Asymmetry, flexibility and sub-complex rotations of the AccA3/AccD4/AccD5/AccE5 holo complex are caused by the presence of a previously unknown epsilon-subunit (AccE5) in red/orange. AccA3, green shades; AccD4, purple shades; AccD5, blue/cyan shades.
We are delighted to share a stunning short/long chain acyl-CoA carboxylase complex with a total of 16 subunits (8 x AccA3, 2 x AccD4, 4 x AccD5, 2 x AccE5). It hosts two related carboxylate transferase subunits (AccD4, AccD5). Our story is now on www.biorxiv.org/content/10.1101/2025.11.15.688623v1
Ensemble model of the full length Pex5 receptor (different blue color) in complex with Pex8 (green colors). Key Findings: Pex8 binds to a novel site on the mostly unfolded N-terminal region of the Pex5 receptor. This interaction is essential for peroxisomal protein import. Computational modelling reveals the formation of an assembly with the trimeric peroxisomal E3-ubiquitin ligase. We propose that this action positions the Pex5 receptor for its recycling, a step essential for the entire protein import process. Why this matters: Peroxisomes rely entirely on the import of folded proteins to function. Impaired peroxisome function is linked to severe disorders, and recent data show their crucial roles in carcinogenesis and the immune response. Our work elevates Pex8 from an enigma to a central player in this critical biological process. Read the full story and see the structures here: https://www.biorxiv.org/content/10.1101/2025.08.30.673231v1 #CellBiology #StructuralBiology #Peroxisome #ProteinImport #bioRxiv #Biochemistry
We are excited to share our latest work, where we unravel the structural and functional secrets of the once-mysterious protein Pex8 revealing how it controls the peroxisomal cargo import receptor Pex5.
Read more here: www.biorxiv.org/content/10.1101/2025.08.30.673231v1
How is nitrogen built into metabolites? Mother nature has invented an amazing set of enzymes, called glutamine amidotransferases, by first generating ammonia and then building it into diverse metabolites. Here is our newest contribution, published in ACS Catalysis doi.org/10.1021/acsc....
