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Structure paper

TitleA Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme beta-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.
Journal, issue, pagesBiochemistry, Vol. 55, Page 5818-5831, Year 2016
Publish dateJun 16, 2016 (structure data deposition date)
AuthorsJasniewski, A.J. / Knoot, C.J. / Lipscomb, J.D. / Que, L.
External linksBiochemistry / PubMed:27668828
MethodsX-ray diffraction
Resolution2.2 - 2.72 Å
Structure data

PDB-5kik:
CmlA beta-hydroxylase in chemically reduced diferrous state
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-5kil:
CmlA beta-hydroxylase E377D mutant
Method: X-RAY DIFFRACTION / Resolution: 2.72 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FEO:
MU-OXO-DIIRON

ChemComp-ACT:
ACETATE ION

Source
  • streptomyces venezuelae (strain atcc 10712 / cbs 650.69 / dsm 40230 / jcm 4526 / nbrc 13096 / pd 04745) (bacteria)
KeywordsMETAL BINDING PROTEIN / Oxygen activation / Diiron cluster / Antibiotic biosynthesis / Beta-hydroxylase / OXIDOREDUCTASE

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