SASDC65: Plasmodium falciparum p23B (Co-chaperone p23, Pfp23B)

基本情報

• 登録情報: データベース: SASBDB / ID: SASDC65

試料

Plasmodium falciparum p23B

• Co-chaperone p23 (protein), Pfp23B, Plasmodium falciparum (isolate 3D7)

機能・相同性

分子機能:

Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / chaperone-mediated protein complex assembly / Hsp90 protein binding / protein folding / protein-folding chaperone binding / nucleus / cytosol

ドメイン・相同性:

CS domain / CS domain / CS domain profile. / HSP20-like chaperone

構成要素:

HSP90 co-chaperone p23

• 生物種: Plasmodium falciparum (isolate 3D7) (マラリア病原虫)
• 引用: ジャーナル: Int J Biol Macromol / 年: 2018; タイトル: Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome.; 著者: Noeli S M Silva / Thiago V Seraphim / Karine Minari / Leandro R S Barbosa / Júlio C Borges / ; 要旨: The p23 proteins are small acidic proteins that aid the functional cycle of the Hsp90 molecular chaperone. Such co-chaperone acts by temporarily inhibiting the ATPase activity of Hsp90 and exhibits intrinsic chaperone activity, suggesting independent roles. A search for p23 in the Plasmodium falciparum genome led to the identification of two putative proteins showing 13% identity to each other and approximately 20% identity to human p23. To understand the presence of two p23 proteins in this organism, we generated recombinant p23 proteins (Pfp23A and Pfp23B) and investigated their structure and function. The proteins presented some similarities and dissimilarities in structural contents and showed different chemical and thermal stabilities, with Pfp23A being more stable than Pfp23B, suggesting that these proteins may present different functions in this organism. Both Pfp23 proteins behaved as elongated monomers in solution and were capable of preventing the thermal-induced aggregation of model client proteins with different efficiencies. Finally, the Pfp23 proteins inhibited the ATPase activity of recombinant P. falciparum Hsp90 (PfHsp90). These results validate the studied proteins as p23 proteins and co-chaperones of PfHsp90.

登録者

• Júlio Borges (Instituto de Química de São Carlos, São Carlos - SP - Brasil)

モデル

• モデル #1317: ; タイプ: dummy / ソフトウェア: (5.0) / ダミー原子の半径: 3.00 A / 対称性: P1 / コメント: Average of 10 models generated by DAMMIN / カイ2乗値: 0.681 / P-value: 0.000835; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Plasmodium falciparum p23B / 試料濃度: 2.00-3.00
• バッファ: 名称: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol; pH: 7.4

要素 #701

名称: Pfp23B / タイプ: protein / 記述: Co-chaperone p23 / 分子量: 30.932 / 分子数: 1 / 由来: Plasmodium falciparum (isolate 3D7) / 参照: UniProt: Q8IKU1
配列:

GSHMQKLYPI VLWAQKKECL YLTIELQDIE NVKIDLKEDK LYFYGTKDKN EYEFTLNFLK PINVEESKYS TQRNIKFKII KKEQERWKTL NNDGKKHWVK CDWNSWVDTD EEDKANDYDD MGMNSFGGMG GMPDMSQFGN MGGLGNMGGL GNMGGLGNMG GLGNMGGLGN MGGLGNMGGL GNMGGMGDLD FSKLGNMGGD MPNFAGLGGM DQFKNMPNMN NMNDDDSSSY GDDTSDEEDD DDEEDEDVEV DNKTLDSDKL KDEENKIPDA AVEVQEPVA

実験情報

• ビーム: 設備名称: Brazilian Synchrotron Light Laboratory SAXS2 Beamline; 地域: Campinas / 国: Brazil / 線源: X-ray synchrotron / 波長: 0.1488 Å / スペクトロメータ・検出器間距離: 1 mm
• 検出器: 名称: MAR 165 CCD

スキャン

タイトル: Plasmodium falciparum p23B / 測定日: 2015年5月26日 / 保管温度: 4 °C / セル温度: 20 °C / 照射時間: 180 sec. / フレーム数: 1 / 単位: 1/nm /

	Min	Max
Q	0.1838	3.1807

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.6 / ポイント数: 235 /

	Min	Max
Q	0.02217	0.3181
P(R) point	4	238
R	0	130

結果

Experimental MW: 32 kDa / カーブのタイプ: merged

	P(R)	P(R) error	Guinier	Guinier error
前方散乱 I0	0.02	0.000479	0.019763	0.0011
慣性半径, Rg	3.97 nm	0.08	3.692 nm	0.3

	Min	Max	Error
D	-	13	5
Guinier point	4	15	-