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TitleOlfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure.
Journal, issue, pagesJ Biol Chem, Vol. 290, Issue 24, Page 15092-15101, Year 2015
Publish dateJun 12, 2015
AuthorsMatti F Pronker / Trusanne G A A Bos / Thomas H Sharp / Dominique M E Thies-Weesie / Bert J C Janssen /
PubMed AbstractOlfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system ...Olfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development. It binds a number of secreted proteins and cell surface-bound receptors to induce cell signaling processes. Using a combined approach of x-ray crystallography, solution scattering, analytical ultracentrifugation, and electron microscopy we determined that full-length Olfm1 forms disulfide-linked tetramers with a distinctive V-shaped architecture. The base of the "V" is formed by two disulfide-linked dimeric N-terminal domains. Each of the two V legs consists of a parallel dimeric disulfide-linked coiled coil with a C-terminal β-propeller dimer at the tips. This agrees with our crystal structure of a C-terminal coiled-coil segment and β-propeller combination (Olfm1(coil-Olf)) that reveals a disulfide-linked dimeric arrangement with the β-propeller top faces in an outward exposed orientation. Similar to its family member myocilin, Olfm1 is stabilized by calcium. The dimer-of-dimers architecture suggests a role for Olfm1 in clustering receptors to regulate signaling and sheds light on the conformation of several other olfactomedin domain family members.
External linksJ Biol Chem / PubMed:25903135 / PubMed Central
MethodsEM (tomography) / X-ray diffraction
Resolution2.4 Å
Structure data

EMDB-2940:
Structural characterization of the Olfactomedin-1 disulfide-linked tetramer
Method: EM (tomography)

EMDB-2941:
Structural characterization of the Olfactomedin-1 disulfide-linked tetramer
Method: EM (tomography)

EMDB-2942:
Structural characterization of the Olfactomedin-1 disulfide-linked tetramer
Method: EM (tomography)

EMDB-2943:
Structural characterization of the Olfactomedin-1 disulfide-linked tetramer
Method: EM (tomography)

EMDB-2944:
Structural characterization of the Olfactomedin-1 disulfide-linked tetramer
Method: EM (tomography)

PDB-5amo:
Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-CL:
Unknown entry / Chloride

ChemComp-HOH:
WATER / Water

Source
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / OLFM1 / DISULFIDE / NEUROBIOLOGY / DEVELOPMENT / AMPA RECEPTOR / BETA PROPELLER

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