SASDFL5: Plasmodium falciparum Hsp70/Hsp90 organizing protein, Hop

Basic information

• Entry: Database: SASBDB / ID: SASDFL5

Sample

Plasmodium falciparum Hsp70/Hsp90 organizing protein, Hop

• STI1-like protein (protein), PfHop, Plasmodium falciparum (isolate 3D7)

Function / homology

Function:

HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Hsp90 protein binding / cytosol

Domain/homology:

STI1/HOP, DP domain / STI1/HOP, DP domain / : / Heat shock chaperonin-binding / Heat shock chaperonin-binding motif. / Tetratricopeptide repeat 1 / Tetratricopeptide repeat / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily

Component:

STI1-like protein

• Biological species: Plasmodium falciparum (isolate 3D7) (eukaryote)
• Citation: Journal: Biochim Biophys Acta Proteins Proteom / Year: 2020; Title: Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities.; Authors: Noeli S M Silva / Dayane E Bertolino-Reis / Paulo R Dores-Silva / Fátima B Anneta / Thiago V Seraphim / Leandro R S Barbosa / Júlio C Borges / ; Abstract: HOP is a cochaperone belonging to the foldosome, a system formed by the cytoplasmic Hsp70 and Hsp90 chaperones. HOP acts as an adapter protein capable of transferring client proteins from the first to the second molecular chaperone. HOP is a modular protein that regulates the ATPase activity of Hsp70 and Hsp90 to perform its function. To obtain more detailed information on the structure and function of this protein, we produced the recombinant HOP of Plasmodium falciparum (PfHOP). The protein was obtained in a folded form, with a high content of α-helix secondary structure. Unfolding experiments showed that PfHOP unfolds through two transitions, suggesting the presence of at least two domains with different stabilities. In addition, PfHOP primarily behaved as an elongated dimer in equilibrium with the monomer. Small-angle X-ray scattering data corroborated this interpretation and led to the reconstruction of a PfHOP ab initio model as a dimer. Finally, the PfHOP protein was able to inhibit and to stimulate the ATPase activity of the recombinant Hsp90 and Hsp70-1, respectively, of P. falciparum. Our results deepened the knowledge of the structure and function of PfHOP and further clarified its participation in the P. falciparum foldosome.

Contact author

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

Models

• Model #2962: ; Type: dummy / Software: (DAMFILT 5.) / Radius of dummy atoms: 3.00 A / Symmetry: P2 / Chi-square value: -1.000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2973: ; Type: dummy / Radius of dummy atoms: 3.00 A / Symmetry: P2 / Chi-square value: -1.000; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Plasmodium falciparum Hsp70/Hsp90 organizing protein, Hop; Specimen concentration: 1.00-2.80
• Buffer: Name: 25 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol; pH: 8

Entity #1620

Name: PfHop / Type: protein / Description: STI1-like protein / Formula weight: 68.219 / Num. of mol.: 2 / Source: Plasmodium falciparum (isolate 3D7) / References: UniProt: Q8ILC1
Sequence:

MGSSHHHHHH SSGLVPRGSH MVNKEEAQRL KELGNKCFQE GKYEEAVKYF SDAITNDPLD HVLYSNLSGA FASLGRFYEA LESANKCISI KKDWPKGYIR KGCAEHGLRQ LSNAEKTYLE GLKIDPNNKS LQDALSKVRN ENMLENAQLI AHLNNIIEND PQLKSYKEEN SNYPHELLNT IKSINSNPMN IRIILSTCHP KISEGVEKFF GFKFTGEGND AEERQRQQRE EEERRKKKEE EERKKKEEEE MKKQNRTPEQ IQGDEHKLKG NEFYKQKKFD EALKEYEEAI QINPNDIMYH YNKAAVHIEM KNYDKAVETC LYAIENRYNF KAEFIQVAKL YNRLAISYIN MKKYDLAIEA YRKSLVEDNN RATRNALKEL ERRKEKEEKE AYIDPDKAEE HKNKGNEYFK NNDFPNAKKE YDEAIRRNPN DAKLYSNRAA ALTKLIEYPS ALEDVMKAIE LDPTFVKAYS RKGNLHFFMK DYYKALQAYN KGLELDPNNK ECLEGYQRCA FKIDEMSKSE KVDEEQFKKS MADPEIQQII SDPQFQIILQ KLNENPNSIS EYIKDPKIFN GLQKLIAAGI LKVR

Experimental information

• Beam: Instrument name: Brazilian Synchrotron Light Laboratory SAXS1 Beamline; City: Campinas / 国: Brazil / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.1488 Å / Dist. spec. to detc.: 0.9 mm
• Detector: Name: Pilatus 300K / Type: 20Hz

Scan

Title: Plasmodium falciparum Hsp70/Hsp90 organizing protein, Hop
Measurement date: Aug 3, 2016 / Cell temperature: 20 °C / Exposure time: 100 sec. / Number of frames: 1 / Unit: 1/A /

	Min	Max
Q	0.0145	0.3252

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 278 /

	Min	Max
Q	0.0144589	0.231278
P(R) point	1	278
R	0	240

Result

Type of curve: extrapolated
Comments: Top: The model represents the averaged spatial disposition (volume and bead-occupancy corrected; damfilt model) obtained from several spatially aligned individual dummy atom model (DAM) reconstructions calculated using DAMMIF. Bottom: A single DAMMIF representative model with the lowest NSD from the aligned DAM cohort. The corresponding fit to the SAXS data is displayed.

	Experimental	Porod
MW	170 kDa	-
Volume	-	557 nm3

	P(R)	Guinier	Guinier error	P(R) error
Forward scattering, I0	0.1399	0.1393	0.0033	-
Radius of gyration, Rg	6.58 nm	6.28 nm	0.15	0.1

	Min	Max	Error
D	-	24	1
Guinier point	3	11	-