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Structure paper

TitleMolecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.
Journal, issue, pagesCell Death Dis, Vol. 8, Page e3119-e3119, Year 2017
Publish dateOct 15, 2016 (structure data deposition date)
AuthorsMerski, M. / Moreira, C. / Abreu, R.M. / Ramos, M.J. / Fernandes, P.A. / Martins, L.M. / Pereira, P.J.B. / Macedo-Ribeiro, S.
External linksCell Death Dis / PubMed:29022916
MethodsX-ray diffraction
Resolution1.649 - 1.9 Å
Structure data

PDB-5m3n:
HTRA2 wild-type structure
Method: X-RAY DIFFRACTION / Resolution: 1.649 Å

PDB-5m3o:
HTRA2 A141S mutant structure
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5tny:
HTRA2 G399S mutant
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5tnz:
HtrA2 S142D mutant
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-5to0:
HTRA2 S276C mutant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5to1:
HtrA2 exposed (L266R, F303A) mutant
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Serine Protease Parkinson Disease Mitochondria PDZ domain Dynamics / Serine Protease / Parkinson Disease / Mitochondria / PDZ Dynamics / Mitochondrial protease / Trimeric Dynamics

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