The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase

Publication Type:
Journal Article
Citation:
Acta Crystallographica Section D: Biological Crystallography, 2011, 67 (2), pp. 105 - 111
Issue Date:
2011-02-01
Metrics:
Full metadata record
Files in This Item:
Filename Description Size
S0907444910051127.pdfPublished Version1.01 MB
Adobe PDF
The Thermus thermophilus protein TTHA0988 is a protein of unknown function which represents a fusion of two proteins found almost ubiquitously across the bacterial kingdom. These two proteins perform a role regulating sporulation in Bacillus subtilis, where they are known as KipI and KipA. kipI and kipA genes are usually found immediately adjacent to each other and are often fused to produce a single polypeptide, as is the case with TTHA0988. Here, three crystal forms are reported of TTHA0988, the first structure to be solved from the family of KipI-KipA fusion proteins. Comparison of the three forms reveals structural flexibility which can be described as a hinge motion between the KipI and KipA components. TTHA0988 is annotated in various databases as a putative allophanate hydrolase. However, no such activity could be identified and genetic analysis across species with known allophanate hydrolases indicates that a misannotation has occurred. © 2011 International Union of Crystallography Printed in Singapore all rights reserved.
Please use this identifier to cite or link to this item: