1BWD

INOSAMINE-PHOSPHATE AMIDINOTRANSFERASE STRB1 FROM STREPTOMYCES GRISEUS

1BWD の概要

• エントリーDOI: 10.2210/pdb1bwd/pdb
• 分子名称: PROTEIN (INOSAMINE-PHOSPHATE AMIDINOTRANSFERASE) (1 entity in total)
• 機能のキーワード: amidinotransferase, streptomycin, transferase
• 由来する生物種: Streptomyces griseus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77477.29

構造登録者

Fritsche, E.,Bergner, A.,Humm, A.,Piepersberg, W.,Huber, R. (登録日: 1998-09-23, 公開日: 1999-01-13, 最終更新日: 2023-08-09)

主引用文献

Fritsche, E.,Bergner, A.,Humm, A.,Piepersberg, W.,Huber, R.
Crystal structure of L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis.
Biochemistry, 37:17664-17672, 1998

PubMed Abstract: Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. L-Arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) was cloned as an N-terminal hexa-histidine fusion protein, purified by affinity chromatography, and crystallized, and its crystal structure was solved by Patterson search methods at 3.1 A resolution. The structure is composed of five betabeta alphabeta-modules which are arranged circularly into a pseudo-5-fold symmetric particle. The three-dimensional structure is closely related to the structure of human L-arginine:glycine amidinotransferase (AT), but five loops (the 40-, 170-, 220-, 250-, and 270-loop) are organized very differently. The major changes are found in loops around the active site which open the narrow active site channel of AT to form an open and solvent-exposed cavity. In particular, module II of StrB1 is AT-like but lacks a 10-residue alpha-helix in the 170-loop. The concomitant reorganization of neighboring surface loops that surround the active site, i.e., the 40-loop and the 270-loop, results in an arrangement of loops which allows an unrestricted access of substrates to the cavity. However, the residues which are involved in substrate binding and catalysis are conserved in AT and StrB1 and are at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases. The binding site for L-arginine had been deduced from its complex with AT. Molecular modeling revealed a possible binding mode for the second substrate scyllo-inosamine 4-phosphate.

PubMed: 9922132
DOI: 10.1021/bi981949p

実験手法

X-RAY DIFFRACTION (3.1 Å)