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Structure paper

TitleAn Intermolecular Binding Mechanism Involving Multiple Lysm Domains Mediates Carbohydrate Recognition by an Endopeptidase.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 71, Page 592-, Year 2015
Publish dateSep 4, 2014 (structure data deposition date)
AuthorsWong, J.E.M.M. / Midtgaard, S.R. / Gysel, K. / Thygesen, M.B. / Sorensen, K.K. / Jensen, K.J. / Stougaard, J. / Thirup, S. / Blaise, M.
External linksActa Crystallogr. ,Sect. D / PubMed:25760608
MethodsX-ray diffraction
Resolution1.75 - 2.65 Å
Structure data

PDB-4uz2:
Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4uz3:
Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4xcm:
Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NDG:
2-acetamido-2-deoxy-alpha-D-glucopyranose

ChemComp-SO4:
SULFATE ION

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

Source
  • thermus thermophilus hb8 (bacteria)
  • thermus thermophilus (bacteria)
KeywordsHYDROLASE / NlpC/P60 / D / L-endopeptidase / LysM domain

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