1LCY	Hydrolase	date	Apr 07, 2002
title	Crystal Structure Of The Mitochondrial Serine Protease Htra2
authors	W.Li, S.M.Srinivasula, J.Chai, P.Li, J.W.Wu, Z.Zhang, E.S.Alnemri, Y.Shi
compound		source
Molecule: Htra2 Serine Protease Chain: A Ec: 3.4.21.- Engineered: Yes Mutation: Yes		Organism_scientific: Homo Sapiens Organism_common: Human Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_plasmid: Pet21b
symmetry	Space Group: H 3	R_factor	0.235
crystal cell	length a length b length c angle alpha angle beta angle gamma 85.420 85.420 127.160 90.00 90.00 120.00
method	X-Ray Diffraction	resolution	2.00 Å
ligand		enzyme	Hydrolase E.C.3.4.21 BRENDA
note	1LCY is a representative structure
domain	The pdz domain mediates interaction with mxi2.
similarity	Belongs to the peptidase s1c family. Contains 1 PDZ (dhr) domain.
subunit	Interacts with mxi2. The mature protein, but not the precursor, binds to birc2, birc3 and birc4/xiap.
post-translat. modifications	Autoproteolytically activated.
tissue	Isoform 1 is ubiquitous; isoform 2 is expressed predominantly in the kidney, colon and thyroid.
subcellular loc.	Membrane localization by OPM: Mitochondrial inner membrane intermembrane space side matrix space side
genes	HTRA2, PRSS25 (H. sapiens)
function	Serine protease that shows proteolytic activity against a nonspecific substrate beta-casein. Isoform 2 seems to be proteolytically inactive. Promotes or induces cell death either by direct binding to and inhibition of birc proteins (also called inhibitor of apoptosis proteins, iaps), leading to an increase in caspase activity, or by a birc inhibition-independent, caspase-independent and serine protease activity-dependent mechanism.
Gene Ontology	Chain Function Process Component A serine-type endopeptidase ac... protein binding peptidase activity serine-type peptidase activi... hydrolase activity unfolded protein binding proteolysis apoptosis response to stress nucleus mitochondrion mitochondrial intermembrane ... endoplasmic reticulum endoplasmic reticulum membra... membrane integral to membrane
disease	Protease,Serine,25; Prss25
Primary reference	Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi., Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y, Nat Struct Biol 2002 Jun;9(6):436-41. PMID:11967569

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (65 Kb) [Save to disk] Biological Unit Coordinates (1lcy.pdb1.gz) 53 Kb CSU: Contacts of Structural Units for 1LCY Likely Quarternary Molecular Structure file(s) for 1LCY Retrieve 1LCY in mmCIF format [Save to disk]

View 1LCY in 3D

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1LCY, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1lcya1, region A:226-325 [Jmol] [rasmolscript] [script source]     - Domain d1lcya2, region A:6-210 [Jmol] [rasmolscript] [script source] Fold representative 1lcy from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1lcy_A]

Other resources with information on 1LCY

InterPro: IPR001940 , IPR001254 , IPR001478 PDBREPORT (protein verification by WHAT_CHECK procedures) MMDB (Entrez's Structure Database)

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