5xtb

Structural highlights

Disease

[NDUS4_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [NDUS7_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [NDUA9_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUS8_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [NDUS6_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUS1_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [NDUS3_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. [NDUV2_HUMAN] Isolated NADH-CoQ reductase deficiency. [NDUV1_HUMAN] Isolated NADH-CoQ reductase deficiency;Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [NDUAD_HUMAN] Papillary or follicular thyroid carcinoma. Disease susceptibility is associated with variations affecting the gene represented in this entry. Defects in NDUFA13 are a cause of a mitochondrial complex I deficiency characterized by early onset hypotonia, dyskinesia and sensorial deficiencies, as well as a severe optic neuropathy.^[1] [NDUAC_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.

Function

[ACPM_HUMAN] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [NDUS4_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^{[2] [3]} [NDUS7_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[4] [NDUA5_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[5] [NDUA9_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^{[6] [7]} [NDUS8_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone. [NDUS6_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[8] [NDUS1_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. [NDUS3_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [NDUV2_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [NDUA7_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[9] [NDUA6_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[10] [NDUV1_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). [NDUAD_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091).^{[11] [12] [13] [14]} [NDUV3_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I.^[15] [NDUAC_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.^[16] [NDUA2_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

References

1. ↑ Angebault C, Charif M, Guegen N, Piro-Megy C, Mousson de Camaret B, Procaccio V, Guichet PO, Hebrard M, Manes G, Leboucq N, Rivier F, Hamel CP, Lenaers G, Roubertie A. Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia and sensorial deficiencies, and mitochondrial complex I instability. Hum Mol Genet. 2015 Jul 15;24(14):3948-55. doi: 10.1093/hmg/ddv133. Epub 2015 Apr, 21. PMID:25901006 doi:http://dx.doi.org/10.1093/hmg/ddv133
2. ↑ Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. PMID:12611891 doi:http://dx.doi.org/10.1074/jbc.C300064200
3. ↑ van den Heuvel L, Ruitenbeek W, Smeets R, Gelman-Kohan Z, Elpeleg O, Loeffen J, Trijbels F, Mariman E, de Bruijn D, Smeitink J. Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am J Hum Genet. 1998 Feb;62(2):262-8. PMID:9463323 doi:http://dx.doi.org/10.1086/301716
4. ↑ Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. PMID:12611891 doi:http://dx.doi.org/10.1074/jbc.C300064200
5. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
6. ↑ van den Bosch BJ, Gerards M, Sluiter W, Stegmann AP, Jongen EL, Hellebrekers DM, Oegema R, Lambrichs EH, Prokisch H, Danhauser K, Schoonderwoerd K, de Coo IF, Smeets HJ. Defective NDUFA9 as a novel cause of neonatally fatal complex I disease. J Med Genet. 2012 Jan;49(1):10-5. doi: 10.1136/jmedgenet-2011-100466. Epub 2011, Nov 23. PMID:22114105 doi:http://dx.doi.org/10.1136/jmedgenet-2011-100466
7. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
8. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
9. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
10. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
11. ↑ Lufei C, Ma J, Huang G, Zhang T, Novotny-Diermayr V, Ong CT, Cao X. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 2003 Mar 17;22(6):1325-35. PMID:12628925 doi:http://dx.doi.org/10.1093/emboj/cdg135
12. ↑ Zhang J, Yang J, Roy SK, Tininini S, Hu J, Bromberg JF, Poli V, Stark GR, Kalvakolanu DV. The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9342-7. Epub 2003 Jul 16. PMID:12867595 doi:http://dx.doi.org/10.1073/pnas.1633516100
13. ↑ Barnich N, Hisamatsu T, Aguirre JE, Xavier R, Reinecker HC, Podolsky DK. GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. J Biol Chem. 2005 May 13;280(19):19021-6. Epub 2005 Mar 7. PMID:15753091 doi:http://dx.doi.org/10.1074/jbc.M413776200
14. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
15. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
16. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
17. ↑ Guo R, Zong S, Wu M, Gu J, Yang M. Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2. Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695 doi:http://dx.doi.org/10.1016/j.cell.2017.07.050