1WD5

Crystal structure of TT1426 from Thermus thermophilus HB8

Summary for 1WD5

• Entry DOI: 10.2210/pdb1wd5/pdb
• Descriptor: hypothetical protein TT1426, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: structural genomics, hypothetical protein, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 22746.64

Authors

Shibata, R.,Kukimoto-Niino, M.,Murayama, K.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-11, release date: 2004-11-11, Last modification date: 2024-11-06)

Primary citation

Kukimoto-Niino, M.,Shibata, R.,Murayama, K.,Hamana, H.,Nishimoto, M.,Bessho, Y.,Terada, T.,Shirouzu, M.,Kuramitsu, S.,Yokoyama, S.
Crystal structure of a predicted phosphoribosyltransferase (TT1426) from Thermus thermophilus HB8 at 2.01 A resolution
Protein Sci., 14:823-827, 2005

PubMed Abstract: TT1426, from Thermus thermophilus HB8, is a conserved hypothetical protein with a predicted phosphoribosyltransferase (PRTase) domain, as revealed by a Pfam database search. The 2.01 A crystal structure of TT1426 has been determined by the multiwavelength anomalous dispersion (MAD) method. TT1426 comprises a core domain consisting of a central five-stranded beta sheet surrounded by four alpha-helices, and a subdomain in the C terminus. The core domain structure resembles those of the type I PRTase family proteins, although a significant structural difference exists in an inserted 43-residue region. The C-terminal subdomain corresponds to the "hood," which contains a substrate-binding site in the type I PRTases. The hood structure of TT1426 differs from those of the other type I PRTases, suggesting the possibility that TT1426 binds an unknown substrate. The structure-based sequence alignment provides clues about the amino acid residues involved in catalysis and substrate binding.

PubMed: 15689504
DOI: 10.1110/ps.041229405

Experimental method

X-RAY DIFFRACTION (2 Å)