7V4Y

TTHA1264/TTHA1265 complex

7V4Y の概要

• エントリーDOI: 10.2210/pdb7v4y/pdb
• 分子名称: Zinc-dependent peptidase, Putative zinc protease, ZINC ION, ... (4 entities in total)
• 機能のキーワード: complex, close conformation, hydrolase
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93900.06

構造登録者

Xu, M.,Xu, Q.,Ran, T.,Wang, W.,Sun, B.,Wang, Q. (登録日: 2021-08-16, 公開日: 2022-06-29, 最終更新日: 2023-11-29)

主引用文献

Xu, M.,Xu, Q.,Wang, M.,Qiu, S.,Xu, D.,Zhang, W.,Wang, W.,He, J.,Wang, Q.,Ran, T.,Sun, B.
Crystal structures of TTHA1265 and TTHA1264/TTHA1265 complex reveal an intrinsic heterodimeric assembly.
Int.J.Biol.Macromol., 207:424-433, 2022

PubMed Abstract: Zinc peptidase M16 family members are widely distributed in most prokaryotic and eukaryotic organisms. M16 family has been divided into three subfamilies, M16A, M16B and M16C, based on sequence alignments and subunit connectivity. TTHA1264, an M16B protein found in Thermus thermophiles HB8, possesses an HXXEH motif essential for Zn binding and catalytic activity. TTHA1265 is another member of M16B, which lacks the metal-binding motif but with a conserved active-site R/Y pair commonly found in the C-terminal half of M16 enzymes. Sequence analysis showed that two genes coding for TTHA1264 and TTHA1265 assemble into a single operon in the bacterial genome. Here, we report the crystal structure of TTHA1265 and TTHA1264/TTHA1265 complex from T. thermophilus HB8. Interestingly, when TTHA1264 and TTHA1265 are present alone, TTHA1264 forms a monomer, TTHA1265 forms a homodimer, respectively. However, TTHA264 and TTHA1265 assembled into a heterodimeric complex, indicating that they prefer to form heterodimer. Biochemical data further confirmed the heterodimeric assembly indicating intrinsic heterodimeric assembly of TTHA1264 and TTHA1265. This property of TTHA1264 and TTHA1265 is consistent with the characteristics of the M16B family.

PubMed: 35276293
DOI: 10.1016/j.ijbiomac.2022.03.020

実験手法

X-RAY DIFFRACTION (2.4 Å)