1WEK

Crystal structure of the conserved hypothetical protein TT1465 from Thermus thermophilus HB8

1WEK の概要

• エントリーDOI: 10.2210/pdb1wek/pdb
• 分子名称: hypothetical protein TT1465, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: rossmann fold, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 147555.24

構造登録者

Kukimoto-Niino, M.,Murayama, K.,Kato-Murayama, M.,Terada, T.,Shirouzu, M.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-05-25, 公開日: 2004-11-25, 最終更新日: 2024-11-20)

主引用文献

Kukimoto-Niino, M.,Murayama, K.,Kato-Murayama, M.,Idaka, M.,Bessho, Y.,Tatsuguchi, A.,Ushikoshi-Nakayama, R.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8
Protein Sci., 13:3038-3042, 2004

PubMed Abstract: TT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical proteins, and are annotated as possible lysine decarboxylases in the Pfam database. Here we report the crystal structures of TT1887 and TT1465 at 1.8 A and 2.2 A resolutions, respectively, as determined by the multiwavelength anomalous dispersion (MAD) method. TT1887 is a homotetramer, while TT1465 is a homohexamer in the crystal and in solution. The structures of the TT1887 and TT1465 monomers contain single domains with the Rossmann fold, comprising six alpha helices and seven beta strands, and are quite similar to each other. The major structural differences exist in the N terminus of TT1465, where there are two additional alpha helices. A comparison of the structures revealed the elements that are responsible for the different oligomerization modes. The distributions of the electrostatic potential on the solvent-accessible surfaces suggested putative active sites.

PubMed: 15459330
DOI: 10.1110/ps.041012404

実験手法

X-RAY DIFFRACTION (2.2 Å)