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TitleStructural Basis for the Catalytic Mechanism of Ethylenediamine- N, N'-disuccinic Acid Lyase, a Carbon-Nitrogen Bond-Forming Enzyme with a Broad Substrate Scope.
Journal, issue, pagesBiochemistry, Vol. 57, Page 3752-3763, Year 2018
Publish dateMar 25, 2018 (structure data deposition date)
AuthorsPoddar, H. / de Villiers, J. / Zhang, J. / Puthan Veetil, V. / Raj, H. / Thunnissen, A.W.H. / Poelarends, G.J.
External linksBiochemistry / PubMed:29741885
MethodsX-ray diffraction
Resolution1.9 - 2.606 Å
Structure data

PDB-6g3d:
Crystal structure of Native EDDS lyase
Method: X-RAY DIFFRACTION / Resolution: 2.221 Å

PDB-6g3e:
Crystal structure of EDDS lyase in complex with formate
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6g3f:
Crystal structure of EDDS lyase in complex with fumarate
Method: X-RAY DIFFRACTION / Resolution: 2.222 Å

PDB-6g3g:
Crystal structure of EDDS lyase in complex with succinate
Method: X-RAY DIFFRACTION / Resolution: 2.606 Å

PDB-6g3h:
Crystal structure of EDDS lyase in complex with SS-EDDS
Method: X-RAY DIFFRACTION / Resolution: 2.269 Å

PDB-6g3i:
Crystal structure of EDDS lyase in complex with N-(2-aminoethyl)aspartic acid (AEAA)
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FMT:
FORMIC ACID

ChemComp-NA:
Unknown entry

ChemComp-FUM:
FUMARIC ACID

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-SIN:
SUCCINIC ACID

ChemComp-EKQ:
(2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid

ChemComp-EKN:
(2~{S})-2-(2-azanylethylamino)butanedioic acid

Source
  • chelativorans sp. (strain bnc1) (bacteria)
KeywordsLYASE / C-N Lyase / metal chelator / EDDS / tetramer / aspartase fumarase superfamily / formate / succinate / AEAA

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