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Structure paper

TitleMolecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 3163, Year 2018
Publish dateAug 8, 2018
AuthorsLuigi Scietti / Antonella Chiapparino / Francesca De Giorgi / Marco Fumagalli / Lela Khoriauli / Solomon Nergadze / Shibom Basu / Vincent Olieric / Lucia Cucca / Blerida Banushi / Antonella Profumo / Elena Giulotto / Paul Gissen / Federico Forneris /
PubMed AbstractLysyl hydroxylases catalyze hydroxylation of collagen lysines, and sustain essential roles in extracellular matrix (ECM) maturation and remodeling. Malfunctions in these enzymes cause severe ...Lysyl hydroxylases catalyze hydroxylation of collagen lysines, and sustain essential roles in extracellular matrix (ECM) maturation and remodeling. Malfunctions in these enzymes cause severe connective tissue disorders. Human lysyl hydroxylase 3 (LH3/PLOD3) bears multiple enzymatic activities, as it catalyzes collagen lysine hydroxylation and also their subsequent glycosylation. Our understanding of LH3 functions is currently hampered by lack of molecular structure information. Here, we present high resolution crystal structures of full-length human LH3 in complex with cofactors and donor substrates. The elongated homodimeric LH3 architecture shows two distinct catalytic sites at the N- and C-terminal boundaries of each monomer, separated by an accessory domain. The glycosyltransferase domain displays distinguishing features compared to other known glycosyltransferases. Known disease-related mutations map in close proximity to the catalytic sites. Collectively, our results provide a structural framework characterizing the multiple functions of LH3, and the molecular mechanisms of collagen-related diseases involving human lysyl hydroxylases.
External linksNat Commun / PubMed:30089812 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.1 - 3 Å
Structure data

SASDDW4:
Procollagen lysyl hydroxylase LH3 measured using SEC-SAXS
Method: SAXS/SANS

PDB-6fxk:
Crystal Structure of full-length Human Lysyl Hydroxylase LH3
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-6fxm:
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Mn2+
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6fxr:
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6fxt:
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Glc
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6fxx:
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal, Hg2+ Soak
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-6fxy:
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal - Structure from long-wavelength S-SAD
Method: X-RAY DIFFRACTION / Resolution: 2.138 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-FE2:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM

ChemComp-HG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Lysyl Hydroxylase / Galacosyltransferase / Glucosyltransferase / Collagen

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