Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain α-ketoacid dehydrogenase complex

Journal of Biological Chemistry

Volumn 286, Issue 26, 2011, Pages 23476-23488

  Brautigam, Chad A ^a   Wynn, R Max ^a   Chuang, Jacinta L ^a   Naik, Mandar T ^b   Young, Brittany B ^a   Huang, Tai Huang ^b,c   Chuang, David T ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b INSTITUTE OF BIOMEDICAL SCIENCES   (Taiwan)

^c NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY INTERACTIONS; BINDING AFFINITIES; BINDING DOMAIN; BINDING REACTIONS; DEHYDROGENASE COMPLEXES; INTERFACIAL AREAS; KETO ACIDS; ORDERS OF MAGNITUDE; OXIDATIVE DECARBOXYLATION; PYRUVATE DEHYDROGENASE COMPLEX; SEQUENCE ALIGNMENTS; SOLUTION NMR; WEAK INTERACTIONS; WILD TYPES;

AMINO ACIDS; BINDING ENERGY; CARBOXYLATION; COMPLEXATION; MAMMALS;

CRYSTAL STRUCTURE;

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); ARGININE; ASPARAGINE; DIHYDROLIPOAMIDE DEHYDROGENASE; ENZYME VARIANT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENTHALPY; ENZYME STRUCTURE; ENZYME SUBUNIT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SEQUENCE ALIGNMENT; STATIC ELECTRICITY; STRUCTURE ANALYSIS; THERMODYNAMICS; WILD TYPE;

AMINO ACID SUBSTITUTION; CRYSTALLOGRAPHY, X-RAY; DIHYDROLIPOAMIDE DEHYDROGENASE; HUMANS; MUTATION, MISSENSE; PROTEIN STRUCTURE, QUATERNARY; STRUCTURE-ACTIVITY RELATIONSHIP;

MAMMALIA;

EID: 79959537557     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.202960     Document Type: Article

References (36)

1. Reed, L. J. (2001) J. Biol. Chem. 276, 38329-38336
2. Yeaman, S. J. (1989) Biochem. J. 257, 625-632
3. Brautigam, C. A., Wynn, R. M., Chuang, J. L., Machius, M., Tomchick, D. R., and Chuang, D. T. (2006) Structure 14, 611-621
4. Jung, H. I., Bowden, S. J., Cooper, A., and Perham, R. N. (2002) Protein Sci. 11, 1091-1100
5. Pettit, F. H., Yeaman, S. J., and Reed, L. J. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 4881-4885
6. Paxton, R., and Harris, R. A. (1982) J. Biol. Chem. 257, 14433-14439
7. Chuang, D. T., Hu, C. C., Ku, L. S., Niu, W. L., Myers, D. E., and Cox, R. P. (1984) J. Biol. Chem. 259, 9277-9284
8. Danner, D. J., and Heffelfinger, S. C. (1988) Methods Enzymol. 166, 298-302
9. Harris, R. A., Bowker-Kinley, M. M., Wu, P., Jeng, J., and Popov, K. M. (1997) J. Biol. Chem. 272, 19746-19751
10. Mande, S. S., Sarfaty, S., Allen, M. D., Perham, R. N., and Hol, W. G. (1996) Structure 4, 277-286
11. Frank, R. A., Pratap, J. V., Pei, X. Y., Perham, R. N., and Luisi, B. F. (2005) Structure 13, 1119-1130
12. Ciszak, E. M., Makal, A., Hong, Y. S., Vettaikkorumakankauv, A. K., Korotchkina, L. G., and Patel, M. S. (2006) J. Biol. Chem. 281, 648-655
13. Brautigam, C. A., Wynn, R. M., Chuang, J. L., and Chuang, D. T. (2009) J. Biol. Chem. 284, 13086-13098
14. Padrick, S. B., Deka, R. K., Chuang, J. L., Wynn, R. M., Chuang, D. T., Norgard, M. V., Rosen, M. K., and Brautigam, C. A. (2010) Anal. Biochem. 407, 89-103
15. Clackson, T., and Wells, J. A. (1995) Science 267, 383-386
16. Bogan, A. A., and Thorn, K. S. (1998) J. Mol. Biol. 280, 1-9
17. Brautigam, C. A., Chuang, J. L., Tomchick, D. R., Machius, M., and Chuang, D. T. (2005) J. Mol. Biol. 350, 543-552
18. Chuang, D. T., Chuang, J. L., and Wynn, R. M. (2006) J. Nutr. 136, 243S-249S
19. Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 859-866
20. Read, R. J. (2001) Acta Crystallogr. D Biol. Crystallogr. 57, 1373-1382
21. Storoni, L. C., McCoy, A. J., and Read, R. J. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 432-438
22. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 486-501
23. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., Mc- Coy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 213-221
24. Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371
25. Goddard, T. D., and Kneller, D. G. (2008) SPARKY 3, University of California, San Francisco
26. Shimada, I. (2005) Methods Enzymol. 394, 483-506
27. Baker, N. A., Sept, D., Joseph, S., Holst, M. J., and McCammon, J. A. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041
28. Lovell, S. C., Word, J. M., Richardson, J. S., and Richardson, D. C. (2000) Proteins 40, 389-408
29. Babady, N. E., Pang, Y. P., Elpeleg, O., and Isaya, G. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 6158-6163
30. Chang, C. F., Chou, H. T., Lin, Y. J., Lee, S. J., Chuang, J. L., Chuang, D. T., and Huang, T. H. (2006) J. Biol. Chem. 281, 28345-28353
31. Cooper, A., Johnson, C. M., Lakey, J. H., and Nöllmann, M. (2001) Biophys. Chem. 93, 215-230
32. Raggett, E. M., Bainbridge, G., Evans, L. J., Cooper, A., and Lakey, J. H. (1998) Mol. Microbiol. 28, 1335-1343
33. DeLano, W. L. (2002) Curr. Opin. Struct. Biol. 12, 14-20
34. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) Nucleic Acids Res. 22, 4673-4680
35. Chen, V. B., Arendall, W. B., 3rd, Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 12-21
36. Harris, R. A., Hawes, J. W., Popov, K. M., Zhao, Y., Shimomura, Y., Sato, J., Jaskiewicz, J., and Hurley, T. D. (1997) Adv. Enzyme Regul. 37, 271-293