4GM2

The crystal structure of a peptidase from plasmodium falciparum

4GM2 の概要

• エントリーDOI: 10.2210/pdb4gm2/pdb
• 分子名称: ATP-dependent Clp protease proteolytic subunit (2 entities in total)
• 機能のキーワード: structural genomics, structural genomics consortium, sgc, protease, hydrolase
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 164035.75

構造登録者

El Bakkouri, M.,Jung, P.,Wernimont, A.K.,Calmettes, C.,Hui, R.,Houry, W.A.,Structural Genomics Consortium (SGC) (登録日: 2012-08-15, 公開日: 2012-12-05, 最終更新日: 2024-02-28)

主引用文献

El Bakkouri, M.,Rathore, S.,Calmettes, C.,Wernimont, A.K.,Liu, K.,Sinha, D.,Asad, M.,Jung, P.,Hui, R.,Mohmmed, A.,Houry, W.A.
Structural Insights into the Inactive Subunit of the Apicoplast-localized Caseinolytic Protease Complex of Plasmodium falciparum.
J.Biol.Chem., 288:1022-1031, 2013

PubMed Abstract: The ATP-dependent caseinolytic protease, ClpP, is highly conserved in bacteria and in the organelles of different organisms. In cyanobacteria, plant plastids, and the apicoplast of the genus Plasmodium, a noncatalytic paralog of ClpP, termed ClpR, has been identified. ClpRs are found to form heterocomplexes with ClpP resulting in a ClpRP tetradecameric cylinder having less than 14 catalytic triads. The exact role of ClpR in such a complex remains enigmatic. Here we describe the x-ray crystal structure of ClpR protein heptamer from Plasmodium falciparum (PfClpR). This is the first structure of a ClpR protein. The structure shows that the PfClpR monomer adopts a fold similar to that of ClpP, but has a unique motif, which we named the R-motif, forming a β turn located near the inactive catalytic triad in a three-dimensional space. The PfClpR heptamer exhibits a more open and flat ring than a ClpP heptamer. PfClpR was localized in the P. falciparum apicoplast as is the case of PfClpP. However, biochemical and structural data suggest that, contrary to what has been observed in other organisms, PfClpP and PfClpR do not form a stable heterocomplex in the apicoplast of P. falciparum.

PubMed: 23192353
DOI: 10.1074/jbc.M112.416560

実験手法

X-RAY DIFFRACTION (2.8 Å)