4NQY

The reduced form of MJ0499

4NQY の概要

• エントリーDOI: 10.2210/pdb4nqy/pdb
• 関連するPDBエントリー: 4kp1 4kp2
• 分子名称: Isopropylmalate/citramalate isomerase large subunit, ZINC ION (3 entities in total)
• 機能のキーワード: alpha-beta sandwitch, isomerase, mj1277, fe-s cluster, cytosol, lyase
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96461.98

構造登録者

Hwang, K.Y.,Lee, E.H.,Lee, K. (登録日: 2013-11-26, 公開日: 2014-05-21, 最終更新日: 2023-11-08)

主引用文献

Lee, E.H.,Lee, K.,Hwang, K.Y.
Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii
Acta Crystallogr.,Sect.D, 70:922-931, 2014

PubMed Abstract: The aconitase family of proteins includes three classes of hydro-lyase enzymes: aconitases, homoaconitases and isopropylmalate (IPM) isomerases. They have a common Fe-S cluster-binding site and catalyze the isomerization of specific substrates by sequential dehydration and hydration. The archaeon Methanococcus jannaschii contains two aconitase family proteins, IPM isomerase and homoaconitase, which have 50% sequence identity. These two enzymes are heterodimeric proteins composed of large and small subunits encoded by separate genes. Although structures have been reported for the small subunits of the two enzymes, the first structures of oxidized and reduced forms of the large subunit of IPM isomerase (ox-MJ0499 and red-MJ0499, respectively) from M. jannaschii are reported here at 1.8 and 2.7 Å resolution, respectively, together with the structure of the large subunit of homoaconitase (MJ1003) at 2.5 Å resolution. The structures of both proteins have unbound Fe-S clusters and contain a fourth cysteine in the active site. The active site of MJ1003 is homologous to that of aconitase, whereas MJ0499 has significant structural distortion at the active site compared with aconitase. In addition, significant large conformational changes were observed in the active site of red-MJ0499 when compared with ox-MJ0499. The active sites of the two proteins adopt two different states before changing to the Fe-S cluster-bound `activated' state observed in aconitase. MJ1003 has an `open' active site, which forms an active pocket for the cluster, while ox-MJ0499 has a `closed' active site, with four cysteines in disulfide bonds. These data will be helpful in understanding the biochemical mechanism of clustering of the Fe-S protein family.

PubMed: 24699638
DOI: 10.1107/S1399004713033762

実験手法

X-RAY DIFFRACTION (2.6 Å)