1MPD

MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG), COMPLEXED WITH MALTOSE

1MPD の概要

• エントリーDOI: 10.2210/pdb1mpd/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: MALTODEXTRIN-BINDING PROTEIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: periplasmic binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P02928
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41066.43

構造登録者

Shilton, B.H.,Mowbray, S.L. (登録日: 1995-07-25, 公開日: 1995-10-15, 最終更新日: 2024-02-14)

主引用文献

Shilton, B.H.,Shuman, H.A.,Mowbray, S.L.
Crystal Structures and Solution Conformations of a Dominant-Negative Mutant of Escherichia Coli Maltose-Binding Protein
J.Mol.Biol., 264:364-376, 1996

PubMed Abstract: A mutant of the periplasmic maltose-binding protein (MBP) with altered transport properties was studied. A change of residue 230 from tryptophan to arginine results in dominant-negative MBP: expression of this protein against a wild-type background causes inhibition of maltose transport. As part of an investigation of the mechanism of such inhibition, we have solved crystal structures of both unliganded and liganded mutant protein. In the closed, liganded conformation, the side-chain of R230 projects into a region of the surface of MBP that has been identified as important for transport while in the open form, the same side-chain takes on a different, and less ordered, conformation. The crystallographic work is supplemented with a small-angle X-ray scattering study that provides evidence that the solution conformation of unliganded mutant is similar to that of wild-type MBP. It is concluded that dominant-negative inhibition of maltose transport must result from the formation of a non-productive complex between liganded-bound mutant MBP and wild-type MalFGK2. A general kinetic framework for transport by either wild-type MalFGK2 or MBP-independent MalFGK2 is used to understand the effects of dominant-negative MBP molecules on both of these systems.

PubMed: 8951382
DOI: 10.1006/jmbi.1996.0646

実験手法

X-RAY DIFFRACTION (2.3 Å)