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Structure paper

TitleCrystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Journal, issue, pagesSci Rep, Vol. 10, Page 5830-5830, Year 2020
Publish dateOct 29, 2019 (structure data deposition date)
AuthorsFellner, M. / Huizenga, K.G. / Hausinger, R.P. / Hu, J.
External linksSci Rep / PubMed:32242052
MethodsX-ray diffraction
Resolution2.39 - 3.55 Å
Structure data

PDB-6utp:
LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with cobalt
Method: X-RAY DIFFRACTION / Resolution: 3.55 Å

PDB-6utq:
LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with cadmium
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

PDB-6utr:
LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with copper
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

PDB-6utt:
LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with calcium
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-CO:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-CD:
Unknown entry

ChemComp-CU:
COPPER (II) ION

ChemComp-CA:
Unknown entry

Source
  • lactobacillus plantarum (bacteria)
KeywordsTRANSFERASE / Lar / sulfur transferase / AMPylation / PP-loop / ATP pyrophophatase domain / lactate racemization / lactate racemase / LarE

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