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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).

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

Cross database links:

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