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9.B.142.5.6
The structure of the yeast O-mannosyltransferase Pmt1-Pmt2 complex has been determined at 3.2 Å resolution (Bai et al. 2019). In eukaryotes, a nascent peptide entering the endoplasmic reticulum (ER) is scanned by two Sec61 translocon-associated large membrane machines for protein N-glycosylation and protein O-mannosylation, respectively. The structures of both the eight-protein oligosaccharyltransferase complex and the mannosyltransferases of the PMT family have been determined.  They function in ER protein homeostasis. Cryo-EM structures of the Saccharomyces cerevisiae Pmt1-Pmt2 complex bound to a donor and an acceptor peptide shows that each subunit contains 11 TMSs and a lumenal beta-trefoil fold termed the MIR domain. The structures reveal the substrate recognition site and confirms an inverting mannosyl-transferring reaction mechanism. The transmembrane domains of Pmt1 and Pmt2 share a structural fold with the catalytic subunits of oligosaccharyltransferases, confirming an evolutionary relationship between protein O-mannosylation and protein N-glycosylation (Bai et al. 2019).

Accession Number:P33775
Protein Name:Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Length:817
Molecular Weight:92675.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:9
Location1 / Topology2 / Orientation3: Endoplasmic reticulum membrane1 / Multi-pass membrane protein2
Substrate

Cross database links:

Structure:
6P25   6P2R     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK LLVACLAVFT 
61:	AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP LAKMLYAGVA SLGGFQGDFD 
121:	FENIGDSFPS TTPYVLMRFF SASLGALTVI LMYMTLRYSG VRMWVALMSA ICFAVENSYV 
181:	TISRYILLDA PLMFFIAAAV YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT 
241:	VTWVGLLCIW RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG 
301:	DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH NYPAGSEQQQ 
361:	STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF HTVTRCRLHS HDHKPPVSES 
421:	SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK NSAPGVAQER VIALDTKFRL RHAMTGCYLF 
481:	SHEVKLPAWG FEQQEVTCAS SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES 
541:	HKKMWHINKN LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF 
601:	GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ MFLHHYLPAY 
661:	YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF FKSFSPIIYG TPWTQELCQK 
721:	SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE SQPAATSTVE EITIEGDGPS YEDLMNEDGK 
781:	KIFKDTEGNE LDPEVVKKML EEEGANILKV EKRAVLE