Structural highlights
Publication Abstract from PubMed
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.
The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase.,Jacques DA, Langley DB, Kuramitsu S, Yokoyama S, Trewhella J, Guss JM Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):105-11. Epub 2011, Jan 8. PMID:21245531[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jacques DA, Langley DB, Kuramitsu S, Yokoyama S, Trewhella J, Guss JM. The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):105-11. Epub 2011, Jan 8. PMID:21245531 doi:10.1107/S0907444910051127
