SASDB54: Leishmania braziliensis stress-induced protein sti1 (LbHop), full...

Basic information

• Entry: Database: SASBDB / ID: SASDB54

Sample

Leishmania braziliensis stress-induced protein sti1 (LbHop), full length construct

• Stress-induced protein sti1 (protein), Hop/Sti1, Leishmania braziliensis

Function / homology

Function:

Hsp70 protein binding / Hsp90 protein binding / protein folding

Domain/homology:

Heat shock protein Sti1-like / STI1/HOP, DP domain / STI1/HOP, DP domain / Heat shock chaperonin-binding / Heat shock chaperonin-binding motif. / Tetratricopeptide repeat 1 / Tetratricopeptide repeat / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily

Component:

Stress-induced protein sti1

• Biological species: Leishmania braziliensis (eukaryote)
• Citation: Journal: Arch Biochem Biophys / Year: 2016; Title: Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis.; Authors: Fernanda A H Batista / Thiago V Seraphim / Clelton A Santos / Marisvanda R Gonzaga / Leandro R S Barbosa / Carlos H I Ramos / Júlio C Borges / ; Abstract: Parasites belonging to the genus Leishmania are subjected to extensive environmental changes during their life cycle; molecular chaperones/co-chaperones act as protagonists in this scenario to maintain cellular homeostasis. Hop/Sti1 is a co-chaperone that connects the Hsp90 and Hsp70 systems, modulating their ATPase activities and affecting the fate of client proteins because it facilitates their transfer from the Hsp70 to the Hsp90 chaperone. Hop/Sti1 is one of the most prevalent co-chaperones, highlighting its importance despite the relatively low sequence identity among orthologue proteins. This multi-domain protein comprises three tetratricopeptides domains (TPR1, TPR2A and TPR2B) and two Asp/Pro-rich domains. Given the importance of Hop/Sti1 for the chaperone system and for Leishmania protozoa viability, the Leishmania braziliensis Hop (LbHop) and a truncated mutant (LbHop(TPR2AB)) were characterized. Structurally, both proteins are α-helix-rich and highly elongated monomeric proteins. Functionally, they inhibited the ATPase activity of Leishmania braziliensis Hsp90 (LbHsp90) to a similar extent, and the thermodynamic parameters of their interactions with LbHsp90 were similar, indicating that TPR2A-TPR2B forms the functional center for the LbHop interaction with LbHsp90. These results highlight the structural and functional similarity of Hop/Sti1 proteins, despite their low sequence conservation compared to the Hsp70 and Hsp90 systems, which are phylogenetic highly conserved.

Contact author

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

Models

• Model #482: ; Type: dummy / Software: DAMFILT / Radius of dummy atoms: 1.90 A / Chi-square value: 3.549; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Leishmania braziliensis stress-induced protein sti1 (LbHop), full length construct; Specimen concentration: 0.80-1.80
• Buffer: Name: Tris / Concentration: 25.00 mM / pH: 7.5 ; Composition: 100 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol

Entity #314

Name: Hop/Sti1 / Type: protein / Description: Stress-induced protein sti1 / Formula weight: 62.452 / Num. of mol.: 1 / Source: Leishmania braziliensis / References: UniProt: A4H5F0
Sequence:

MDANELKNEG NKEFSAGRYV EAVNYFSKAI QLDGQNSVLY SNRSACFAAM QKYKDALDDA DKCISIKPNW AKGYVRRGAA LHGMRRYDDA IAAYEKGLSV DPSNSGCTQG VKDVQVAKSR EARDPIARVF TPEAFRKIQE NPKLSLLMLQ PDYVKMVDTV VRDPSQARLY MEDQRFALTL MYLSGMKIPN DDEDDEEERP SAKAAAEAKA KEEKKLLTDN EKEAMALKEE GNKLYLSKRF EEALSKYQEA QAKDPKNTLY ILNVSAVYFE QRDYEKCITE CERGIEHGRE NHCDYTIVAK LMTRHAFCLQ KQKKYEAAID LYKRALVEWR NPDTLKKLTE CEKEHQKAVE EAYIDPEIAR QKKDEGNQYF KEDKFPEAVA AYTEAIKRNP AEHTSYSNRA AAYIKLGAFN DALKDAEKCI ELKPDFVKGY ARKGHAYFWT KQYNRALQAY DEGLKVDPSN ADCKDGRLRT IMRIQEMASG QSADGDEAAR RAMDDPEIAA IMQDSYMQLV LKEMQNDPTR IQEYMKDPGI SVKINKLISA GIIRFGQ

Experimental information

• Beam: Instrument name: Brazilian Synchrotron Light Laboratory SAXS1 Beamline; City: Campinas / 国: Brazil / Type of source: X-ray synchrotronSynchrotron
• Detector: Name: Pilatus 300K / Type: 20Hz

Scan

Title: Stress-induced protein sti1 (Hop/Sti1) / Measurement date: Feb 21, 2016 / Unit: 1/nm /

	Min	Max
Q	0.1235	4.067

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 497 /

	Min	Max
Q	0.01235	0.4067
P(R) point	1	497
R	0	180

Result

Type of curve: merged /

	Experimental	Porod
MW	63 kDa	59 kDa
Volume	-	94 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.0632	0.0002	0.063	-
Radius of gyration, Rg	4.68 nm	0.02	4.51 nm	0.05

	Min	Max
D	-	18
Guinier point	3	16