6D71

Crystal Structure of the Human Miro1 N-terminal GTPase bound to GTP

6D71 の概要

• エントリーDOI: 10.2210/pdb6d71/pdb
• 分子名称: Mitochondrial Rho GTPase 1, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: gtpase, mitochondria, miro, rho, gem1p, calcium, gtp, kinesin, mom, transport protein
• 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: 43709.36

構造登録者

Smith, K.P.,Focia, P.J.,Rice, S.E.,Freymann, D.M. (登録日: 2018-04-23, 公開日: 2019-10-09, 最終更新日: 2024-05-22)

主引用文献

Smith, K.P.,Focia, P.J.,Chakravarthy, S.,Landahl, E.C.,Klosowiak, J.L.,Rice, S.E.,Freymann, D.M.
Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.
J.Struct.Biol., 212:107656-107656, 2020

PubMed Abstract: Dysfunction in mitochondrial dynamics is believed to contribute to a host of neurological disorders and has recently been implicated in cancer metastasis. The outer mitochondrial membrane adapter protein Miro functions in the regulation of mitochondrial mobility and degradation, however, the structural basis for its roles in mitochondrial regulation remain unknown. Here, we report a 1.7Å crystal structure of N-terminal GTPase domain (nGTPase) of human Miro1 bound unexpectedly to GTP, thereby revealing a non-catalytic configuration of the putative GTPase active site. We identify two conserved surfaces of the nGTPase, the "SELFYY" and "ITIP" motifs, that are potentially positioned to mediate dimerization or interaction with binding partners. Additionally, we report small angle X-ray scattering (SAXS) data obtained from the intact soluble HsMiro1 and its paralog HsMiro2. Taken together, the data allow modeling of a crescent-shaped assembly of the soluble domain of HsMiro1/2. PDB RSEFERENCE: Crystal structure of the human Miro1 N-terminal GTPase bound to GTP, 6D71.

PubMed: 33132189
DOI: 10.1016/j.jsb.2020.107656

実験手法

X-RAY DIFFRACTION (1.71807785325 Å)