3ORE

Crystal structure of TTHA0988 in space group P6522

3ORE の概要

• エントリーDOI: 10.2210/pdb3ore/pdb
• 関連するPDBエントリー: 3OEP 3OPF
• 分子名称: Putative uncharacterized protein TTHA0988 (1 entity in total)
• 機能のキーワード: kipi, kipa, cyclophilin, allophanate hydrolase, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function, nppsfa, national project on protein structural and functional analyses
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106314.78

構造登録者

Jacques, D.A.,Kuramitsu, S.,Yokoyama, S.,Trewhella, J.,Guss, J.M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2010-09-07, 公開日: 2011-02-02, 最終更新日: 2024-03-20)

主引用文献

Jacques, D.A.,Langley, D.B.,Kuramitsu, S.,Yokoyama, S.,Trewhella, J.,Guss, J.M.
The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase
Acta Crystallogr.,Sect.D, 67:105-111, 2011

PubMed Abstract: 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.

PubMed: 21245531
DOI: 10.1107/S0907444910051127

実験手法

X-RAY DIFFRACTION (2.9 Å)