1AX3

SOLUTION NMR STRUCTURE OF B. SUBTILIS IIAGLC, 16 STRUCTURES

1AX3 の概要

• エントリーDOI: 10.2210/pdb1ax3/pdb
• 分子名称: GLUCOSE PERMEASE IIA DOMAIN (1 entity in total)
• 機能のキーワード: phosphotransferase system, sugar transport, transferase, phosphorylation, transmembrane
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P20166
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17396.79

構造登録者

Chen, Y.,Case, D.A.,Reizer, J.,Saier Junior, M.H.,Wright, P.E. (登録日: 1997-10-25, 公開日: 1998-06-17, 最終更新日: 2024-05-22)

主引用文献

Chen, Y.,Case, D.A.,Reizer, J.,Saier Jr., M.H.,Wright, P.E.
High-resolution solution structure of Bacillus subtilis IIAglc.
Proteins, 31:258-270, 1998

PubMed Abstract: The high-resolution solution structure of the phosphocarrier protein IIAglc from Bacillus subtilis is determined using 3D and 4D heteronuclear NMR methods. B. subtilis IIAglc contains 162 amino acid residues and is one of the larger proteins for which high-resolution solution structure has been determined by NMR methods. The structures have been calculated from a total of 2,232 conformational constraints. Comparison with the X-ray crystal structure indicates that the overall fold is the same in solution and in crystalline environments, although some local structural differences are observed. These occur largely in turns and loops, and mostly correspond to regions with high-temperature factors in the crystal structure. The N-terminus of IIAglc is disordered in solution. The active site is located in a concave region of the protein surface. The histidine, which accepts the phosphoryl group (His 83), interacts with a neighboring histidine (His 68) and is surrounded by hydrophobic residues.

PubMed: 9593197
DOI: 10.1002/(SICI)1097-0134(19980515)31:3<258::AID-PROT3>3.3.CO;2-Q

実験手法

SOLUTION NMR