5B89

Crystal structure of a Cysteine Desulfurase from Thermococcus onnurineus NA1 in complex with alanine at 1.5 Angstrom resolution

Summary for 5B89

• Entry DOI: 10.2210/pdb5b89/pdb
• Related: 5B87
• Descriptor: Cysteine desulfurase, ALANINE, PYRIDOXAL-5'-PHOSPHATE, ... (6 entities in total)
• Functional Keywords: cysteine desulfurase, l-cysteine sulfur-transferase, transferase
• Biological source: Thermococcus onnurineus (strain NA1)
• Total number of polymer chains: 2
• Total formula weight: 94235.12

Authors

Ho, T.-H.,Kang, L.-W. (deposition date: 2016-06-13, release date: 2017-06-14, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)