3NDP

Crystal structure of human AK4(L171P)

3NDP の概要

• エントリーDOI: 10.2210/pdb3ndp/pdb
• 分子名称: Adenylate kinase isoenzyme 4, SULFATE ION (3 entities in total)
• 機能のキーワード: parallel beta-sheet, alpha-helices, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion matrix : P27144
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53486.78

構造登録者

Liu, R.,Wang, Y.,Wei, Z.,Gong, W. (登録日: 2010-06-07, 公開日: 2010-06-23, 最終更新日: 2024-04-03)

主引用文献

Liu, R.,Xu, H.,Wei, Z.,Wang, Y.,Lin, Y.,Gong, W.
Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion
Biochem.Biophys.Res.Commun., 379:92-97, 2009

PubMed Abstract: It is well known that motion of LID and NMP-binding (NMP(bind)) domains in adenylate kinase (AK) is important in ligand binding and catalysis. However, the nature of such domain motions is poorly characterized. One of the critical hinge regions is hinge IV, which connects the CORE and LID domains. In addition, the hinge IV contains a strictly conserved residue, L171, in the AK family. To investigate the role of hinge IV, crystal structure of human adenylate kinase 4 (AK4) L171P mutant was determined. This mutation dramatically changes the orientation of the LID domain, which could be described as a novel twisted-and-closed conformation in contrast to the open and closed conformations in other AKs. This mutant provides a new example of domain motions in AK family.

PubMed: 19073142
DOI: 10.1016/j.bbrc.2008.12.012

実験手法

X-RAY DIFFRACTION (2.3 Å)