3OPF

Crystal structure of TTHA0988 in space group P212121

Summary for 3OPF

• Entry DOI: 10.2210/pdb3opf/pdb
• Related: 3OEP
• Descriptor: Putative uncharacterized protein TTHA0988, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: kipi, kipa, cyclophilin, allophanate hydrolase, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function, nppsfa, national project on protein structural and functional analyses
• Biological source: Thermus thermophilus
• Total number of polymer chains: 3
• Total formula weight: 160128.74

Authors

Jacques, D.A.,Kuramitsu, S.,Yokoyama, S.,Trewhella, J.,Guss, J.M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2010-09-01, release date: 2011-02-02, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.95 Å)