5VGR

Human Atlastin-3, GDP-bound

5VGR の概要

• エントリーDOI: 10.2210/pdb5vgr/pdb
• 分子名称: Atlastin-3, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: g proteins, gtpase, membrane fusion, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99235.57

構造登録者

O'Donnell, J.P.,Sondermann, H. (登録日: 2017-04-11, 公開日: 2017-05-17, 最終更新日: 2023-10-04)

主引用文献

O'Donnell, J.P.,Cooley, R.B.,Kelly, C.M.,Miller, K.,Andersen, O.S.,Rusinova, R.,Sondermann, H.
Timing and Reset Mechanism of GTP Hydrolysis-Driven Conformational Changes of Atlastin.
Structure, 25:997-1010.e4, 2017

PubMed Abstract: The endoplasmic reticulum (ER) forms a branched, dynamic membrane tubule network that is vital for cellular function. Branching arises from membrane fusion facilitated by the GTPase atlastin (ATL). Many metazoan genomes encode for three ATL isoforms that appear to fulfill partially redundant function despite differences in their intrinsic GTPase activity and localization within the ER; however, the underlying mechanistic differences between the isoforms are poorly understood. Here, we identify discrete temporal steps in the catalytic cycle for the two most dissimilar isoforms, ATL1 and ATL3, revealing an overall conserved progression of molecular events from nucleotide binding and hydrolysis to ATL dimerization and phosphate release. A crystal structure of ATL3 suggests a mechanism for the displacement of the catalytic Mg ion following guanosine triphosphate (GTP) hydrolysis. Together, the data extend the mechanistic framework for how GTP hydrolysis drives conformational changes in ATL and how the cycle is reset for subsequent rounds of catalysis.

PubMed: 28602821
DOI: 10.1016/j.str.2017.05.007

実験手法

X-RAY DIFFRACTION (2.096 Å)