5B7U

Apo Structure of Cysteine Desulfurase from Thermococcus onnurineus NA1 at 1.89A

5B7U の概要

• エントリーDOI: 10.2210/pdb5b7u/pdb
• 関連するPDBエントリー: 5B7S
• 分子名称: Cysteine desulfurase, CYSTEINE, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: cysteine desulfurylase transferases, l-cysteine, iron sulfur cluster, transferase
• 由来する生物種: Thermococcus onnurineus (strain NA1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94045.98

構造登録者

Ho, T.-H.,Kang, L.-W. (登録日: 2016-06-09, 公開日: 2017-06-14, 最終更新日: 2023-11-15)

主引用文献

Ho, T.-H.,Huynh, K.-H.,Nguyen, D.Q.,Park, H.,Jung, K.,Sur, B.,Ahn, Y.-J.,Cha, S.-S.,Kang, L.-W.
Catalytic Intermediate Crystal Structures of Cysteine Desulfurase from the ArchaeonThermococcus onnurineus NA1.
Archaea, 2017:5395293-5395293, 2017

PubMed Abstract: NA1 is an anaerobic archaeon usually found in a deep-sea hydrothermal vent area, which can use elemental sulfur (S) as a terminal electron acceptor for energy. Sulfur, essential to many biomolecules such as sulfur-containing amino acids and cofactors including iron-sulfur cluster, is usually mobilized from cysteine by the pyridoxal 5'-phosphate- (PLP-) dependent enzyme of cysteine desulfurase (CDS). We determined the crystal structures of CDS from NA1 (ToCDS), which include native internal aldimine (NAT), gem-diamine (GD) with alanine, internal aldimine structure with existing alanine (IAA), and internal aldimine with persulfide-bound Cys356 (PSF) structures. The catalytic intermediate structures showed the dihedral angle rotation of Schiff-base linkage relative to the PLP pyridine ring. The ToCDS structures were compared with bacterial CDS structures, which will help us to understand the role and catalytic mechanism of ToCDS in the archaeon NA1.

PubMed: 28536498
DOI: 10.1155/2017/5395293

実験手法

X-RAY DIFFRACTION (1.9 Å)