1B32

OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KMK

1B32 の概要

• エントリーDOI: 10.2210/pdb1b32/pdb
• 分子名称: PROTEIN (OLIGO-PEPTIDE BINDING PROTEIN), PROTEIN (LYS-MET-LYS), URANYL (VI) ION, ... (5 entities in total)
• 機能のキーワード: complex (peptide transport-peptide), peptide transport, peptide binding protein
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61860.09

構造登録者

Tame, J.R.H.,Wilkinson, A.J. (登録日: 1998-12-15, 公開日: 1998-12-23, 最終更新日: 2023-08-09)

主引用文献

Sleigh, S.H.,Seavers, P.R.,Wilkinson, A.J.,Ladbury, J.E.,Tame, J.R.
Crystallographic and calorimetric analysis of peptide binding to OppA protein.
J.Mol.Biol., 291:393-415, 1999

PubMed Abstract: Isothermal titration calorimetry has been used to study the binding of 20 different peptides to the peptide binding protein OppA, and the crystal structures of the ligand complexes have been refined. This periplasmic binding protein, part of the oligopeptide permease system of Gram negative bacteria, has evolved to bind and enclose small peptides of widely varying sequences. The peptides used in this study have the sequence Lys-X-Lys, where X is any of the 20 commonly occurring amino acids. The various side-chains found at position 2 on the ligand fit into a hydrated pocket. The majority of side-chains are restrained to particular conformations within the pocket. Water molecules act as flexible adapters, matching the hydrogen-bonding requirements of the protein and ligand and shielding charges on the buried ligand. This use of water by OppA to broaden the repertoire of its binding site is not unique, but contrasts sharply with other proteins which use water to help bind ligands highly selectively. Predicting the thermodynamics of binding from the structure of the complexes is highly complicated by the influence of water on the system.

PubMed: 10438628
DOI: 10.1006/jmbi.1999.2929

実験手法

X-RAY DIFFRACTION (1.75 Å)