4HVK

Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.

4HVK の概要

• エントリーDOI: 10.2210/pdb4hvk/pdb
• 関連するPDBエントリー: 4EB5 4EB7
• 分子名称: Probable cysteine desulfurase 2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: transferase and iscs, transferase
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44194.62

構造登録者

Yamanaka, Y.,Zeppieri, L.,Nicolet, Y.,Marinoni, E.N.,de Oliveira, J.S.,Masafumi, O.,Dean, D.R.,Fontecilla-Camps, J.C. (登録日: 2012-11-06, 公開日: 2012-12-05, 最終更新日: 2024-02-28)

主引用文献

Yamanaka, Y.,Zeppieri, L.,Nicolet, Y.,Marinoni, E.N.,de Oliveira, J.S.,Odaka, M.,Dean, D.R.,Fontecilla-Camps, J.C.
Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.
Dalton Trans, 42:3092-3099, 2013

PubMed Abstract: L-Cysteine desulfurase IscS and scaffold IscU proteins are universally involved in Fe/S cluster synthesis. The Archaeoglobus fulgidus (Af) genome encodes proteins having a high degree of primary structure similarity to IscS and IscU from other organisms. However, AfIscS is unusual because it lacks the active site lysine residue that normally forms an internal Schiff base with pyridoxal-phosphate (PLP) and serves as a base during catalysis. Our as-isolated recombinant AfIscS contains pyridoxamine phosphate (PMP) instead of the expected PLP and lacks desulfurase activity. We have solved its structure to 1.43 Å resolution and found that PMP binds non-covalently at the PLP site of the enzyme and displays significant disorder. However, the previously reported structure of recombinant Af(IscU-D35A-IscS)(2) contains an in vivo generated [Fe(2)S(2)] species within AfIscU and the question arises as to how its sulfides were generated. Here, we report that adding PLP to AfIscS produces an enzyme that displays in vitro L-cysteine desulfurase activity mediating the synthesis of a stable holo Af(IscU-D35A-IscS) complex.

PubMed: 23160436
DOI: 10.1039/c2dt32101g

実験手法

X-RAY DIFFRACTION (1.43 Å)