4WB0

Crystal structure of the broad specificity aminotransferase from Leishmania mexicana

4WB0 の概要

• エントリーDOI: 10.2210/pdb4wb0/pdb
• 分子名称: Broad specificity aminotransferase, CACODYLATE ION, ... (4 entities in total)
• 機能のキーワード: transamination, broad specificity, pyridoxal phosphate, transferase
• 由来する生物種: Leishmania mexicana; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93199.75

構造登録者

Wen, J.,Nowicki, C.,Blankenfeldt, W. (登録日: 2014-09-02, 公開日: 2015-09-09, 最終更新日: 2024-11-06)

主引用文献

Wen, J.,Nowicki, C.,Blankenfeldt, W.
Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferase.
Mol.Biochem.Parasitol., 202:34-37, 2015

PubMed Abstract: Leishmania species are early branching eukaryotic parasites that cause difficult-to-treat tissue-damaging diseases known as leishmaniases. As a hallmark of their parasitic lifestyle, Leishmaniae express a number of aminotransferases that are involved in important cellular processes and exhibit broader substrate specificity than their mammalian host's counterparts. Here, we have determined the crystal structure of the broad specificity aminotransferase from Leishmania mexicana (LmexBSAT) at 1.91Å resolution. LmexBSAT is a homodimer and belongs to the α-branch of family-I aminotransferases. Despite the fact that the protein was crystallized in the absence of substrates and has lost the pyridoxal-5'-phosphate (PLP) cofactor during crystallization, the structure resembles the closed, ligand-bound form of related enzymes such as chicken cytosolic aspartate aminotransferase. Its broader substrate specificity seems to be rooted in increased flexibility of a substrate-binding arginine (R291) and the interactions of this residue with the N-terminus of the second chain of the dimer.

PubMed: 26456583
DOI: 10.1016/j.molbiopara.2015.09.007

実験手法

X-RAY DIFFRACTION (1.91 Å)