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Structure paper

TitleStructural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold.
Journal, issue, pagesMol. Microbiol., Vol. 98, Page 289-301, Year 2015
Publish dateDec 26, 2014 (structure data deposition date)
AuthorsWang, P. / Chen, X.L. / Li, C.Y. / Gao, X. / Zhu, D.Y. / Xie, B.B. / Qin, Q.L. / Zhang, X.Y. / Su, H.N. / Zhou, B.C. ...Wang, P. / Chen, X.L. / Li, C.Y. / Gao, X. / Zhu, D.Y. / Xie, B.B. / Qin, Q.L. / Zhang, X.Y. / Su, H.N. / Zhou, B.C. / Xun, L.Y. / Zhang, Y.Z.
External linksMol. Microbiol. / PubMed:26154071
MethodsX-ray diffraction
Resolution1.949 - 2.1 Å
Structure data

PDB-4rzy:
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP in complex with MES
Method: X-RAY DIFFRACTION / Resolution: 1.949 Å

PDB-4rzz:
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP in complex with phosphate
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4s00:
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP mutant Y366A in complex with acrylate
Method: X-RAY DIFFRACTION / Resolution: 2.099 Å

PDB-4s01:
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP mutant D377N in complex with acrylate
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-AKR:
ACRYLIC ACID

Source
  • silicibacter lacuscaerulensis (bacteria)
  • silicibacter lacuscaerulensis iti-1157 (bacteria)
KeywordsLYASE / metallopeptidase-like DMSP lyase / DMSP lyase / metallopeptidase-like

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