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1.B.1.7.2
Sugar-specific chitoporin of 375 aas, ChiP.  The best substrate is chitohexose, but ChiP  transports a variety of chitooligosaccharides.  Trp136 is important for the binding affinity for chitohexaose (Chumjan et al. 2015). X-ray crystal structures of ChiP from V. harveyi in the presence and absence of chito-oligosaccharides have been solved (Aunkham et al. 2018). Structures without bound sugar reveal a trimeric assembly with an unprecedented closing of the transport pore by the N-terminus of a neighboring subunit. Substrate binding ejects the pore plug to open the transport channel.The structures explain the exceptional affinity of ChiP for chito-oligosaccharides and point to an important role of the N-terminal gate in substrate transport (Aunkham et al. 2018). Hydrogen-bonds contribute to sugar permeation (Chumjan et al. 2019). This protein is 90% identical to the chitoporin of the Vibrio campbellii chitoporin (Aunkham et al. 2020). The C2 entity of chitosugars is crucial for the molecular selectivity of the Vibrio campbellii chitoporin (Suginta et al. 2021).

Accession Number:L0RVU0
Protein Name:Chitoporin
Length:375
Molecular Weight:41089.00
Species:Vibrio harveyi [669]
Number of TMSs:1
Substrate

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Structure:
5MDO   5MDP   5MDQ   5MDR   5MDS     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MASYLKKSLL ATAITGMMFS GSAFADGANS DAAKEYLTKD SFSYEVYGII AMQAAYRDYD 
61:	SGDAKQDDNL GGMQLNNESR IGFRGKKQFA NFEPTFIWQI EGGYVDPSFG GEGAGLGERD 
121:	TFVGFESASW GQVRLGRVLT PMYELVDWPA SNPGLGDVYD WGGAIGGAKY QDRQSNTIRW 
181:	DSPMYADKFS IDAAVGAGDK AGLGAGDDYW GGIAAHYKLG PLQLDAAYEG NRNIEAEGQT 
241:	WENNTYLVGV QGWFENGISF FAQYKYMEAD ASNGVNEKQD AMSAGLMYTT GDWQYKLGYA 
301:	ANFDLERDGK TLSNTSDDVV SAQIMYFVDP SAVLYARARM NDFNEGLDGL DDAARWTSGT 
361:	NGDYNEYSVG VEYYF