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Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases

Carbohydrate esterases alter polysaccharides by removing ester groups. Here, the authors resolved crystal structures of two CE20 enzymes and discovered a novel, water-mediated catalytic triad essential for activity, offering insights into enzyme function and mechanism.

Michelle Teune
Plínio S. Vieira
Uwe T. Bornscheuer
ResearchOpen Access31 Jul 2025
Nature Communications

Volume: 16, P: 1-13
The structural basis for spectral variations in green fluorescent protein

Based on structures of five mutants of green fluorescent protein (GFP), we describe two conformational variants with differing charge distribution that explain the published absorption and fluorescence spectra of GFP mutants.

Gottfried J. Palm
Alexander Zdanov
Alexander Wlodawer
Correspondence01 May 1997
Nature Structural Biology

Volume: 4, P: 361-365
Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate

Plastic polymer PET degrading enzymes are of great interest for achieving sustainable plastics recycling. Here, the authors present the crystal structures of the plastic degrading bacterial enzymes PETase, MHETase in its apo-form and MHETase bound to a non-hydrolyzable substrate analog.

Gottfried J. Palm
Lukas Reisky
Gert Weber
ResearchOpen Access12 Apr 2019
Nature Communications

Volume: 10, P: 1-10
Distribution and diversity of classical deacylases in bacteria

In bacteria Zn2+-dependent deacylases are underexplored. Here, the authors identify bacterial deacylases, providing systemic structure-function analyses to reveal the basis of substrate specificity, acyl-chain preference and inhibition.

Leonie G. Graf
Carlos Moreno-Yruela
Michael Lammers
ResearchOpen Access03 Nov 2024
Nature Communications

Volume: 15, P: 1-31
Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule

AMP-forming acetyl-CoA synthetase (AcsA) is an essential enzyme in all domains of life. Here, the authors provide mechanistic insights into regulation of AcsA by lysine acetylation, uncovering a regulatory phosphotransacetylase activity.

Chuan Qin
Leonie G. Graf
Michael Lammers
ResearchOpen Access17 Jul 2024
Nature Communications

Volume: 15, P: 1-22
DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis

DYW domains catalyse cytidine deamination in plant RNA editing, but information on their structure and mode of action were lacking. Now, crystal structures of the DYW domain are reported and a gating domain, key catalytic residues and an unusual protein regulation mechanism are revealed.

Mizuki Takenaka
Sachi Takenaka
Gert Weber
ResearchOpen Access21 Jun 2021
Nature Catalysis

Volume: 4, P: 510-522
Lipolysis-derived fatty acids are needed for homeostatic control of sterol element-binding protein-1c driven hepatic lipogenesis

Fatty acids released by ATGL in adipose tissue inhibit post-translational activation of SREBP1c in the liver. We propose that this ATGL/SREBP-1c axis adds an additional layer of coordination between lipolysis and lipogenesis.

Paola Peña de la Sancha
Beatrix Irene Wieser
Paul Willibald Vesely
ResearchOpen Access09 Apr 2025
Communications Biology

Volume: 8, P: 1-14
Bacteria employ lysine acetylation of transcriptional regulators to adapt gene expression to cellular metabolism

The mechanisms underlying adaptation of bacteria to changing environmental conditions remain poorly understood. Here, the authors show bacteria using lysine acetylation of transcriptional regulators to adjust gene expression to changing conditions.

Magdalena Kremer
Sabrina Schulze
Michael Lammers
ResearchOpen Access23 Feb 2024
Nature Communications

Volume: 15, P: 1-25

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Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases

The structural basis for spectral variations in green fluorescent protein

Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate

Distribution and diversity of classical deacylases in bacteria

Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule

DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis

Lipolysis-derived fatty acids are needed for homeostatic control of sterol element-binding protein-1c driven hepatic lipogenesis

Bacteria employ lysine acetylation of transcriptional regulators to adapt gene expression to cellular metabolism

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