3ASB

Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis

3ASB の概要

• エントリーDOI: 10.2210/pdb3asb/pdb
• 関連するPDBエントリー: 3ASA
• 分子名称: LL-diaminopimelate aminotransferase (2 entities in total)
• 機能のキーワード: plp dependent aminotransferase, transferase
• 由来する生物種: Chlamydia trachomatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44940.76

構造登録者

Watanabe, N.,James, M.N. (登録日: 2010-12-10, 公開日: 2011-08-31, 最終更新日: 2025-03-26)

主引用文献

Watanabe, N.,Clay, M.D.,van Belkum, M.J.,Fan, C.,Vederas, J.C.,James, M.N.
The Structure of ll-Diaminopimelate Aminotransferase from Chlamydia trachomatis: Implications for Its Broad Substrate Specificity.
J.Mol.Biol., 411:649-660, 2011

PubMed Abstract: We have previously reported the structures of the native holo and substrate-bound forms of LL-diaminopimelate aminotransferase from Arabidopsis thaliana (AtDAP-AT). Here, we report the crystal and molecular structures of the LL-diaminopimelate aminotransferase from Chlamydia trachomatis (CtDAP-AT) in the apo-form and the pyridoxal-5'-phosphate-bound form. The molecular structure of CtDAP-AT shows that its overall fold is essentially identical with that of AtDAP-AT except that CtDAP-AT adopts an "open" conformation as opposed to the "closed" conformation of AtDAP-AT. Although AtDAP-AT and CtDAP-AT are approximately 40% identical in their primary sequence, they have major differences in their substrate specificities; AtDAP-AT is highly specific for LL-DAP, whereas CtDAP-AT accepts a wider range of substrates. Since all of the residues involved in substrate recognition are highly conserved between AtDAP-AT and CtDAP-AT, we propose that differences in flexibility of the loops lining the active-site region between the two enzymes likely account for the differences in substrate specificity.

PubMed: 21722650
DOI: 10.1016/j.jmb.2011.06.023

実験手法

X-RAY DIFFRACTION (2.7 Å)