The structure of a crenarchaeal mannosyltransferase displays a minimal cellulose-synthase-like fold:
Gandini R, Reichenbach T, Spadiut O, Tan TC, Kalyani DC, Divne C (2020) A transmembrane crenarchaeal mannosyltransferase is involved in N-glycan biosynthesis and displays an unexpected minimal cellulose-synthase-like fold. J Mol Biol 432:4658

Acne-causing bacterium can feed on host N-glycans:
Reichenbach T, Kalyani DC, Gandini R, Svartström O, Aspeborg H, Divne C (2018) Structural and biochemical characterization of theCutibacterium acnes exo-β-1,4-mannosidase that targets theN-glycan core of host glycoproteins. PLoS One13:e0204703
KTH Press release in Swedish
Ciennce Press release in Swedish
KTH Press release in English

Deciphering the mechanism of synthesis of the glycolipid precursor for N-glycan biosynthesis by the integral membrane protein DPMS:
Gandini R, Reichenbach T, Tan TC & Divne C (2017) Structural basis for dolichylphosphate mannose biosynthesis. Nature Communications8:120
KTH press release in Swedish
KTH press release in English

The CDH-PMO system for oxidative cellulose degradation confirmed by high-resolution crystal structures:
Tan TCet al & Divne C (2015) Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation. Nature Communications 6:7542
KTH press release in Swedish

Light at the end of a cellulose-binding tunnel:
Divne Cet al & Jones TA (1998) High-resolution crystal structures reveal how a cellulose chain is bound in the 50Å long tunnel of cellobiohydrolase I fromTrichoderma reesei. J Mol Biol 275:309 (citations: 343; ave.citations per year: 14)

Our seminal paper in Science on the structural basis of degradation of crystalline cellulose:
Divne Cet al & Jones TA (1994) The three-dimensional structure of the catalytic core of cellobiohydrolase I fromTrichoderma reesei. Science 265:524 (citations: 520; ave.citations per year: 18)

Funding agencies

Swedish Research Council VR, grant No. 2017-03877, 2018-2021
Swedish Research Council Formas, grant No. 2017-00983, 2018-2020
Stiftelsen Oscar och Lili Lamms Minne, grant No. DO2017-0020, 2018-2021

Bibliometry
Publications: 62
Google Scholar citations: 5569
Google Scholars H-index: 34
i10 index: 54

Research scope

My research scope is to understand how enzymes work that enable reactions involving sugar molecules in biological systems.We study enzymes that synthesize, degrade and modify carbohydrates using protein X-ray crystallography and cryo-electron microscopy in conjunction with molecular biology, biochemistry and biophysics techniques.

None

The cellulose-degrading enzyme CBH1 bound to the surface of crystalline cellulose and processively hydrolyzing a cellulose chain.

Glycan and glycolipid synthases

Despite the general importance of sugar biopolymers to organism biology, little is known about the molecular details of their synthesis. We are interested in the molecular mechanisms underlying biogenesis of glycoconjugates and polysaccharides important to life. We use state-of-the-art tools in membrane protein molecular biology, biochemistry and structural biology. Examples of enzymes under study are glycosyltransferases (GTs) that are integral multipass transmembrane proteins with varying topological complexity, and mainly reactions where donor sugars are transferred to a lipid or sugar acceptor. The systems currently under study include N-glycan, ganglioside and polysaccharide biosynthesis.

Besides increasing the fundamental knowledge about the natural biological processes, important aims also include discovery and design of transmembrane GTs that can be used for cell-free in-vitro production of glycoconjugates and polysaccharides for advanced and controlled biomaterial design and therapeutics.

Carbohydrate-active enzymes in host-pathogen interactions

Within this scope, we are particularly interested in understanding the pathways and mechanisms of enzymes that synthesize and modify phytopathogenic polysaccharides and flavonoids, as well as enzymes of commensal bacteria involved in natural, health-promoting interactions with the human host.