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Structure paper

TitleRole of the nucleotidyl cyclase helical domain in catalytically active dimer formation.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page E9821-E9828, Year 2017
Publish dateJun 2, 2017 (structure data deposition date)
AuthorsVercellino, I. / Rezabkova, L. / Olieric, V. / Polyhach, Y. / Weinert, T. / Kammerer, R.A. / Jeschke, G. / Korkhov, V.M.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:29087332
MethodsX-ray diffraction
Resolution2.7 - 3.4 Å
Structure data

PDB-5o5k:
X-ray structure of a bacterial adenylyl cyclase soluble domain
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

PDB-5o5l:
X-ray structure of a bacterial adenylyl cyclase soluble domain, solved at cryogenic temperature
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-ONM:
3'-O-(N-METHYLANTHRANILOYL)-GUANOSINE-5'-TRIPHOSPHATE

ChemComp-MN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • mycobacterium intracellulare 1956 (bacteria)
KeywordsMEMBRANE PROTEIN / membrane-integral adenylyl cyclase / helical domain / catalytic domain / MANT-GTP

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