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TitleCrystal Structure of Escherichia coli Diaminopropionate Ammonia-lyase Reveals Mechanism of Enzyme Activation and Catalysis
Journal, issue, pagesJ. Biol. Chem., Vol. 287, Page 20369-20381, Year 2012
Publish dateJan 11, 2012 (structure data deposition date)
AuthorsBisht, S. / Rajaram, V. / Bharath, S.R. / Kalyani, J.N. / Khan, F. / Rao, A.N. / Savithri, H.S. / Murthy, M.R.N.
External linksJ. Biol. Chem. / PubMed:22505717
MethodsX-ray diffraction
Resolution2 - 2.5 Å
Structure data

PDB-4d9g:
Crystal structure of Selenomethionine incorporated holo Diaminopropionate ammonia lyase from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-4d9i:
Crystal structure of holo Diaminopropionate ammonia lyase from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4d9k:
Crystal structure of Escherichia coli Diaminopropionate ammonia lyase in apo form
Method: X-RAY DIFFRACTION / Resolution: 2.19 Å

PDB-4d9m:
Crystal structure of Diaminopropionate ammonia lyase from Escherichia coli in complex with aminoacrylate-PLP azomethine reaction intermediate
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4d9n:
Crystal structure of Diaminopropionate ammonia lyase from Escherichia coli in complex with D-serine
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-0JO:
2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid

ChemComp-DSN:
D-SERINE

Source
  • escherichia coli (E. coli)
KeywordsLYASE / Fold type II PLP-dependent enzyme / Tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily / S-hydroxyethylation of cysteine

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