Baumann, Ulrich (2019). Structure-Function Relationships of the Repeat Domains of RTX Toxins. Toxins, 11 (11). BASEL: MDPI. ISSN 2072-6651

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Abstract

RTX proteins are a large family of polypeptides of mainly Gram-negative origin that are secreted into the extracellular medium by a type I secretion system featuring a non-cleavable C-terminal secretion signal, which is preceded by a variable number of nine-residue tandem repeats. The three-dimensional structure forms a parallel beta-roll, where beta-strands of two parallel sheets are connected by calcium-binding linkers in such a way that a right-handed spiral is built. The Ca2+ ions are an integral part of the structure, which cannot form without them. The structural determinants of this unique architecture will be reviewed with its conservations and variations together with the implication for secretion and folding of these proteins. The general purpose of the RTX domains appears to act as an internal chaperone that keeps the polypeptide unfolded in the calcium-deprived cytosol and triggers folding in the calcium-rich extracellular medium. A rather recent addition to the structural biology of the RTX toxin is a variant occurring in a large RTX adhesin, where this non-canonical beta-roll binds to ice and diatoms.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Baumann, UlrichUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-128865
DOI: 10.3390/toxins11110657
Journal or Publication Title: Toxins
Volume: 11
Number: 11
Date: 2019
Publisher: MDPI
Place of Publication: BASEL
ISSN: 2072-6651
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
PERTUSSIS ADENYLATE-CYCLASE; CRYSTAL-STRUCTURE; PSEUDOMONAS-AERUGINOSA; ERWINIA-CHRYSANTHEMI; ALKALINE PROTEASE; ESCHERICHIA-COLI; I SECRETION; SERRATIA SP; PROTEINS; METALLOPROTEASEMultiple languages
Food Science & Technology; ToxicologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/12886

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