2O0T

The three dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation

2O0T の概要

• エントリーDOI: 10.2210/pdb2o0t/pdb
• 関連するPDBエントリー: 1HKV 1HKW
• 分子名称: Diaminopimelate decarboxylase, SULFATE ION (3 entities in total)
• 機能のキーワード: plp binding enzyme, decarboxylase, lysine biosynthesis, structural genomics, tb structural genomics consortium, tbsgc, lyase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 199805.39

構造登録者

Weyand, S.,Kefala, G.,Weiss, M.S.,TB Structural Genomics Consortium (TBSGC) (登録日: 2006-11-28, 公開日: 2007-02-13, 最終更新日: 2023-11-15)

主引用文献

Weyand, S.,Kefala, G.,Svergun, D.I.,Weiss, M.S.
The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation.
J Struct Funct Genomics, 10:209-217, 2009

PubMed Abstract: The three-dimensional structure of the enzyme diaminopimelate decarboxylase from Mycobacterium tuberculosis has been determined in a new crystal form and refined to a resolution of 2.33 A. The monoclinic crystals contain one tetramer exhibiting D(2)-symmetry in the asymmetric unit. The tetramer exhibits a donut-like structure with a hollow interior. All four active sites are accessible only from the interior of the tetrameric assembly. Small-angle X-ray scattering indicates that in solution the predominant oligomeric species of the protein is a dimer, but also that higher oligomers exist at higher protein concentrations. The observed scattering data are best explained by assuming a dimer-tetramer equilibrium with about 7% tetramers present in solution. Consequently, at the elevated protein concentrations in the crowded environment inside the cell the observed tetramer may constitute the biologically relevant functional unit of the enzyme.

PubMed: 19543810
DOI: 10.1007/s10969-009-9065-z

実験手法

X-RAY DIFFRACTION (2.33 Å)