3NZI

Substrate induced remodeling of the active site regulates HtrA1 activity

Summary for 3NZI

• Entry DOI: 10.2210/pdb3nzi/pdb
• Related: 3NUM 3NWU
• Descriptor: Serine protease HTRA1, Citrate synthase (2 entities in total)
• Functional Keywords: serine protease, degp, htra, protease, hydrolase-peptide inhibitor complex, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane : Q92743
• Total number of polymer chains: 2
• Total formula weight: 37535.77

Authors

Truebestein, L.,Tennstaedt, A.,Hauske, P.,Krojer, T.,Kaiser, M.,Clausen, T.,Ehrmann, M. (deposition date: 2010-07-16, release date: 2011-02-23, Last modification date: 2024-11-20)

Primary citation

Truebestein, L.,Tennstaedt, A.,Monig, T.,Krojer, T.,Canellas, F.,Kaiser, M.,Clausen, T.,Ehrmann, M.
Substrate-induced remodeling of the active site regulates human HTRA1 activity.
Nat.Struct.Mol.Biol., 18:386-388, 2011

PubMed Abstract: Crystal structures of active and inactive conformations of the human serine protease HTRA1 reveal that substrate binding to the active site is sufficient to stimulate proteolytic activity. HTRA1 attaches to liposomes, digests misfolded proteins into defined fragments and undergoes substrate-mediated oligomer conversion. In contrast to those of other serine proteases, the PDZ domain of HTRA1 is dispensable for activation or lipid attachment, indicative of different underlying mechanistic features.

PubMed: 21297635
DOI: 10.1038/nsmb.2013

Experimental method

X-RAY DIFFRACTION (2.75 Å)