Crystal structure of Icp55 from Saccharomyces cerevisiae (N-terminal 42 residues deletion)

Crystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic function.

Intermediate cleaving peptidase of 55 kDa

GSAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPN
SVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNP
SSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSF
LHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVL
NVQRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVI
TIEPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

100mM HEPES pH 7.5, 22 % Peg3350 , 250mM Ammonium Sulphate, 0.2mM MnCl2

On Superdex200, elutes at a volume which corresponds to molecular mass of 74 kDa (equillibration between monomer and dimer). PISA analysis suggests monomeric nature of protein

Intermediate cleaving peptidase 55, M24B, peptidase, Xaa-Pro aminopeptidase, mitochondrial, HYDROLASE

AGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSV
MILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSS
SNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLH
YKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVLNV
QRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITI
EPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL