2H5A

Complex of the enzyme PMM/PGM with xylose 1-phosphate

2H5A の概要

• エントリーDOI: 10.2210/pdb2h5a/pdb
• 関連するPDBエントリー: 1K2y 1K35 1P5D 1P5g 1pcj 1pcm 2H4L
• 分子名称: Phosphomannomutase/phosphoglucomutase, ZINC ION, 1-O-phosphono-alpha-D-xylopyranose, ... (4 entities in total)
• 機能のキーワード: enzyme-ligand complex, inhibitor, isomerase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50753.90

構造登録者

Regni, C.,Shackelford, G.S.,Beamer, L.J. (登録日: 2006-05-25, 公開日: 2006-08-08, 最終更新日: 2024-11-06)

主引用文献

Regni, C.,Shackelford, G.S.,Beamer, L.J.
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
Acta Crystallogr.,Sect.F, 62:722-726, 2006

PubMed Abstract: Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.

PubMed: 16880541
DOI: 10.1107/S1744309106025887

実験手法

X-RAY DIFFRACTION (1.72 Å)