1FNM

STRUCTURE OF THERMUS THERMOPHILUS EF-G H573A

1FNM の概要

• エントリーDOI: 10.2210/pdb1fnm/pdb
• 分子名称: ELONGATION FACTOR G, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: bent conformation, visible domain iii, mutation his573ala, translation
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm: P13551
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77377.54

構造登録者

Laurberg, M.,Kristensen, O.,Martemyanov, K.,Gudkov, A.T.,Nagaev, I.,Hughes, D.,Liljas, A. (登録日: 2000-08-22, 公開日: 2000-11-22, 最終更新日: 2024-02-07)

主引用文献

Laurberg, M.,Kristensen, O.,Martemyanov, K.,Gudkov, A.T.,Nagaev, I.,Hughes, D.,Liljas, A.
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.
J.Mol.Biol., 303:593-603, 2000

PubMed Abstract: The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EF-G domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.

PubMed: 11054294
DOI: 10.1006/jmbi.2000.4168

実験手法

X-RAY DIFFRACTION (2.8 Å)