PDBsum entry 1s3a

Oxidoreductase

PDB id

1s3a

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Contents

			Protein chain

					85 a.a. *

* Residue conservation analysis

PDB id:

1s3a

Links
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Name:

Oxidoreductase

Title:

Nmr solution structure of subunit b8 from human nadh-ubiquinone oxidoreductase complex i (ci-b8)

Structure:

Nadh-ubiquinone oxidoreductase b8 subunit. Chain: a. Synonym: complex i-b8, ci-b8. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ndufa2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

19 models

Authors:

C.Brockmann,A.Diehl,K.Rehbein,R.Kuhne,H.Oschkinat

Key ref:

C.Brockmann et al. (2004). The oxidized subunit B8 from human complex I adopts a thioredoxin fold. Structure, 12, 1645-1654. PubMed id: 15341729 DOI: 10.1016/j.str.2004.06.021

Date:

13-Jan-04

Release date:

25-Jan-05

PROCHECK

	Headers

	References

Protein chain

O43678 (NDUA2_HUMAN) - NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 from Homo sapiens

Seq: Struc:					99 a.a. 85 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class 2:

E.C.1.6.5.3 - Transferred entry: 7.1.1.2.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

NADH + ubiquinone + 5 H⁺(In) = NAD⁺ + ubiquinol + 4 H(+)(Out)

NADH	+	ubiquinone	+	5 × H(+)(In)	=	NAD(+)	+	ubiquinol	+	4 × H(+)(Out)

Cofactor:

FMN; Iron-sulfur

FMN	Iron-sulfur

Enzyme class 3:

E.C.1.6.99.3 - Deleted entry.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

NADH + acceptor = NAD⁺ + reduced acceptor

NADH	+	acceptor	=	5 × NAD(+)	+	reduced acceptor

Cofactor:

Flavoprotein; Iron-sulfur

Flavoprotein	Iron-sulfur

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2004.06.021	Structure 12:1645-1654 (2004)
PubMed id: 15341729

The oxidized subunit B8 from human complex I adopts a thioredoxin fold.
C.Brockmann, A.Diehl, K.Rehbein, H.Strauss, P.Schmieder, B.Korn, R.Kühne, H.Oschkinat.

ABSTRACT

Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I.

Selected figure(s)



	Figure 3. Figure 3. Relaxation Rate Measurements and Amount of Interresidue NOEs per Residue(A) This panel shows the distribution of NOE-based interresidue restraints on the sequence of CI-B8.(B) This panel shows the 15N-T1/T[2] ratios for each amino acid.

Figure was selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19366614

V.Zickermann, S.Kerscher, K.Zwicker, M.A.Tocilescu, M.Radermacher, and U.Brandt (2009).
Architecture of complex I and its implications for electron transfer and proton pumping.

Biochim Biophys Acta, 1787, 574-583.

18513682

S.J.Hoefs, C.E.Dieteren, F.Distelmaier, R.J.Janssen, A.Epplen, H.G.Swarts, M.Forkink, R.J.Rodenburg, L.G.Nijtmans, P.H.Willems, J.A.Smeitink, and L.P.van den Heuvel (2008).
NDUFA2 complex I mutation leads to Leigh disease.

Am J Hum Genet, 82, 1306-1315.

16319061

A.D.Ferguson, V.M.Labunskyy, D.E.Fomenko, D.Araç, Y.Chelliah, C.A.Amezcua, J.Rizo, V.N.Gladyshev, and J.Deisenhofer (2006).
NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.

J Biol Chem, 281, 3536-3543.

PDB codes:

2a2p 2a4h

16756485

U.Brandt (2006).
Energy converting NADH:quinone oxidoreductase (complex I).

Annu Rev Biochem, 75, 69-92.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.