1PC3

Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis.

1PC3 の概要

• エントリーDOI: 10.2210/pdb1pc3/pdb
• 分子名称: Phosphate-binding protein 1, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: phosphate transport receptor, immonodominant antigen, mycobacterium tuberculosis, ion-dipole interactions, electrostatics, transport protein
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cell membrane; Lipid-anchor (Probable): P15712
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71831.50

構造登録者

Vyas, N.K.,Vyas, M.N.,Quiocho, F.A. (登録日: 2003-05-15, 公開日: 2004-05-18, 最終更新日: 2023-08-16)

主引用文献

Vyas, N.K.,Vyas, M.N.,Quiocho, F.A.
Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions.
Structure, 11:765-774, 2003

PubMed Abstract: The 2.16 A structure of the phosphate-bound PstS-1, the primary extracellular receptor for the ABC phosphate transporter and immunodominant species-specific antigen of Mycobacterium tuberculosis, has been determined. The phosphate, completely engulfed in the cleft between two domains, is bound by 13 hydrogen bonds, 11 of which are formed with NH and OH dipolar donor groups. The further presence of two acidic residues, which serve as acceptors of the protonated phosphate, is key to conferring stringent specificity. The ion-dipole interactions between the phosphate and dipolar groups compensate the ligand's isolated negative charges. Moreover, the surprise finding that the electrostatic surface in and around the cleft is intensely negative demonstrates the power of ion-dipole interactions in anion binding and electrostatic balance. Additional functional features include both the flexible N-terminal segment that tethers PstS-1 on the cell surface and the hinge between the two domains, which should facilitate snaring the phosphate in the medium.

PubMed: 12842040
DOI: 10.1016/S0969-2126(03)00109-6

実験手法

X-RAY DIFFRACTION (2.16 Å)