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TitleFunctional and structural characterization of methionine gamma-lyases from Brevibacterium bacteria: insights into cofactor retention
Journal, issue, pagesTo Be Published
Publish dateNov 12, 2024 (structure data deposition date)
AuthorsFerchaud, N. / Boyer, A. / Odegard, B. / Hentati, S. / Simonson, T. / Machover, D. / Kopecny, D. / Briozzo, P.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.522 - 3.238 Å
Structure data

PDB-9hde:
Crystal structure of methionine gamma-lyase (K209Q variant) from Brevibacterium aurantiacum in complex with PLP and alpha-ketobutyrate
Method: X-RAY DIFFRACTION / Resolution: 2.522 Å

PDB-9hee:
Crystal structure of methionine gamma-lyase from Brevibacterium aurantiacum having disordered N-terminus and devoid of PLP cofactor
Method: X-RAY DIFFRACTION / Resolution: 3.238 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-SO4:
SULFATE ION

ChemComp-4LM:
(2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid

ChemComp-HOH:
WATER

Source
  • brevibacterium aurantiacum (bacteria)
KeywordsLYASE / Complex / inhibitor / methionine / PLP / Apoform

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