BMRB Entry 17067

Name: Complex hMia40-hCox17
Published: 2010-11-15

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PDB ID: 2l0y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17067
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Complex hMia40-hCox17

Deposition date:

2010-07-20

Original release date:

2010-11-15

Authors:

Bertini, Ivano; Ciofi-Baffoni, Simone; Gallo, Angelo

Citation:

Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Cenacchi, Lucia; Ciofi-Baffoni, Simone; Felli, Isabella Caterina; Gallo, Angelo; Gonnelli, Leonardo; Luchinat, Enrico; Sideris, Dionisia; Tokatlidis, Kostas. "Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import." Proc. Natl. Acad. Sci. U.S.A. 107, 20190-20195 (2010).
PubMed: 21059946

Assembly members:

Assembly members:
Mia40, polymer, 146 residues, 6727.517 Da.
Cox17, polymer, 67 residues, 2412.846 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDEST-His-MBP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mia40: GSFTMSYCRQEGKDRIIFVT KEDHETPSSAELVADDPNDP YEEHGLILPNGNINWNSPCL GGMASGPCGEQFKSAFSCFH YSTEEIKGSDCVDQFRAMQE CMQKYPDLYPQEDEDEEEER EKKPAEQAEETAPIEATATK EEEGSS
Cox17: GSFTMPGLVDSNPAPPESQE KKPLKPCCASPETKKARDAS IIEKGEEHCGHLIEAHKESM RALGFKI

Data sets:

assigned_chemical_shifts
- Mia40_cs

Data type	Count
13C chemical shifts	526
15N chemical shifts	148
1H chemical shifts	461

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mia40	1
2	Cox17	2

Entities:

Entity 1, Mia40 146 residues - 6727.517 Da.

1

GLY

SER

PHE

THR

MET

SER

TYR

CYS

ARG

GLN

2

GLU

GLY

LYS

ASP

ARG

ILE

PHE

VAL

THR

3

LYS

GLU

ASP

HIS

GLU

THR

PRO

SER

ALA

4

GLU

LEU

VAL

ALA

ASP

PRO

ASN

ASP

PRO

5

TYR

GLU

HIS

GLY

LEU

ILE

LEU

PRO

ASN

6

GLY

ASN

ILE

ASN

TRP

ASN

SER

PRO

CYS

LEU

7

GLY

MET

ALA

SER

GLY

PRO

CYS

GLY

GLU

8

GLN

PHE

LYS

SER

ALA

PHE

SER

CYS

PHE

HIS

9

TYR

SER

THR

GLU

ILE

LYS

GLY

SER

ASP

10

CYS

VAL

ASP

GLN

PHE

ARG

ALA

MET

GLN

GLU

11

CYS

MET

GLN

LYS

TYR

PRO

ASP

LEU

TYR

PRO

12

GLN

GLU

ASP

GLU

ASP

GLU

ARG

13

GLU

LYS

PRO

ALA

GLU

GLN

ALA

GLU

14

THR

ALA

PRO

ILE

GLU

ALA

THR

ALA

THR

LYS

15

GLU

GLY

SER

Entity 2, Cox17 67 residues - 2412.846 Da.

1

GLY

SER

PHE

THR

MET

PRO

GLY

LEU

VAL

ASP

2

SER

ASN

PRO

ALA

PRO

GLU

SER

GLN

GLU

3

LYS

PRO

LEU

LYS

PRO

CYS

ALA

SER

4

PRO

GLU

THR

LYS

ALA

ARG

ASP

ALA

SER

5

ILE

GLU

LYS

GLY

GLU

HIS

CYS

GLY

6

HIS

LEU

ILE

GLU

ALA

HIS

LYS

GLU

SER

MET

7

ARG

ALA

LEU

GLY

PHE

LYS

ILE

Samples:

sample_1: Mia40, [U-100% 13C; U-100% 15N], 0.5 mM; Cox17 0.5 mM; Phosphate 50 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_2: Cox17, [U-100% 13C; U-100% 15N], 0.5 mM; Mia40 0.5 mM; Phosphate 50 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D ω1- 13C-edited, ω2-13C-filtered NOESY	sample_1	isotropic	sample_conditions_1
3D ω1- 13C-edited, ω2-13C-filtered NOESY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v2, Keller and Wuthrich - chemical shift assignment, data analysis

AMBER v10.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 500 MHz

BMRB	15763 17821
PDB	2K3J 2L0Y 2LGQ
DBJ	BAB71132 BAF83453
GB	AAH17082 AAH33775 AIC53061 EAW64180 EAW64181
REF	NP_001091972 NP_001185638 NP_653237 XP_001157417 XP_002813171
SP	Q8N4Q1
AlphaFold	Q8N4Q1