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Structure paper

TitleStructural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.
Journal, issue, pagesPlos Pathog., Vol. 10, Page e1004109-e1004109, Year 2014
Publish dateJan 24, 2014 (structure data deposition date)
AuthorsGu, J. / Feng, Y. / Feng, X. / Sun, C. / Lei, L. / Ding, W. / Niu, F. / Jiao, L. / Yang, M. / Li, Y. ...Gu, J. / Feng, Y. / Feng, X. / Sun, C. / Lei, L. / Ding, W. / Niu, F. / Jiao, L. / Yang, M. / Li, Y. / Liu, X. / Song, J. / Cui, Z. / Han, D. / Du, C. / Yang, Y. / Ouyang, S. / Liu, Z.J. / Han, W.
External linksPlos Pathog. / PubMed:24831957
MethodsNMR (solution) / X-ray diffraction
Resolution2.27 - 2.694 Å
Structure data

PDB-2mk5:
Solution structure of a protein domain
Method: SOLUTION NMR

PDB-4olk:
The CHAP domain of LysGH15
Method: X-RAY DIFFRACTION / Resolution: 2.694 Å

PDB-4ols:
The amidase-2 domain of LysGH15
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-B3P:
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-FE:
Unknown entry

Source
  • staphylococcus phage gh15 (virus)
KeywordsHYDROLASE / CHAP / amidase-2 domain

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