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-基本情報
登録情報 | データベース: SASBDB / ID: SASDC85 |
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試料 | Leishmania braziliensis p23B
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機能・相同性 | CS domain / CS domain / CS domain profile. / HSP20-like chaperone / Contig, possible fusion of chromosomes 20 and 34 機能・相同性情報 |
生物種 | Leishmania braziliensis (ブラジルリーシュマニア) |
引用 | ジャーナル: FEBS J / 年: 2015 タイトル: Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. 著者: Fernanda A H Batista / Glessler S Almeida / Thiago V Seraphim / Kelly P Silva / Silvane M F Murta / Leandro R S Barbosa / Júlio C Borges / 要旨: The small acidic protein called p23 acts as a co-chaperone for heat-shock protein of 90 kDa (Hsp90) during its ATPase cycle. p23 proteins inhibit Hsp90 ATPase activity and show intrinsic chaperone ...The small acidic protein called p23 acts as a co-chaperone for heat-shock protein of 90 kDa (Hsp90) during its ATPase cycle. p23 proteins inhibit Hsp90 ATPase activity and show intrinsic chaperone activity. A search for p23 in protozoa, especially trypanosomatids, led us to identify two putative proteins in the Leishmania braziliensis genome that share approximately 30% identity with each other and with the human p23. To understand the presence of two p23 isoforms in trypanosomatids, we obtained the recombinant p23 proteins of L. braziliensis (named Lbp23A and Lbp23B) and performed structural and functional studies. The recombinant proteins share similar solution structures; however, temperature- and chemical-induced unfolding experiments showed that Lbp23A is more stable than Lbp23B, suggesting that they may have different functions. Lbp23B prevented the temperature-induced aggregation of malic dehydrogenase more efficiently than did Lbp23A, whereas the two proteins had equivalent efficiencies with respect to preventing the temperature-induced aggregation of luciferase. Both proteins interacted with L. braziliensis Hsp90 (LbHsp90) and inhibited its ATPase activity, although their efficiencies differed. In vivo identification studies suggested that both proteins are present in L. braziliensis cells grown under different conditions, although Lbp23B may undergo post-translation modifications. Interaction studies indicated that both Lbp23 proteins interact with LbHsp90. Taken together, our data suggest that the two protozoa p23 isoforms act similarly when regulating Hsp90 function. However, they also have some differences, indicating that the L. braziliensis Hsp90 machine has features providing an opportunity for novel forms of selective inhibition of protozoan Hsp90. |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #1324 | タイプ: dummy / ソフトウェア: (5.0) / 対称性: P1 / カイ2乗値: 2.829124 / P-value: 0.000054 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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-試料
試料 | 名称: Leishmania braziliensis p23B / 試料濃度: 1.00-4.00 |
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バッファ | 名称: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol / pH: 8 |
要素 #707 | 名称: Lbp23B / タイプ: protein / 記述: Leishmania braziliensis p23 isoform B / 分子量: 23.045 / 分子数: 1 / 由来: Leishmania braziliensis / 参照: UniProt: A4HAD9 配列: GSHMSASGSL VPPISWAQRP EYVLVTIPLQ DTTGVTVEIK DEGRELLFAC CAPEGKQYAC TIHFYGAISS EESQHVVRPR QIELKLRKKL TRSLEDADDE VEWPRLTKEK VKYPNITIDW SKWKDEDDEG ATDDLGDFGL GGGDAMDGQY SEMLSQLMQT QGKKDAEELA ...配列: GSHMSASGSL VPPISWAQRP EYVLVTIPLQ DTTGVTVEIK DEGRELLFAC CAPEGKQYAC TIHFYGAISS EESQHVVRPR QIELKLRKKL TRSLEDADDE VEWPRLTKEK VKYPNITIDW SKWKDEDDEG ATDDLGDFGL GGGDAMDGQY SEMLSQLMQT QGKKDAEELA GLPPGTIPEF GSAQRQEATH GASAAAGDDD SEMPPLEDDM |
-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 | |||||||||||||||||||||||||||
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検出器 | 名称: MAR 165 CCD | |||||||||||||||||||||||||||
スキャン | タイトル: Leishmania braziliensis p23B / 測定日: 2012年3月26日 / 保管温度: 4 °C / セル温度: 20 °C / 照射時間: 300 sec. / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 4.5a / ポイント数: 248 /
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結果 | Experimental MW: 26 kDa / カーブのタイプ: single_conc
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