Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 18, 2014, Pages 6630-6635

  Zhao, Aiguo ^a,b   Fang, Ying ^a,b   Chen, Xuemin ^a,b   Zhao, Shun ^a,b   Dong, Wei ^a,b   Lin, Yajing ^c   Gong, Weimin ^c   Liu, Lin ^a  

^a INSTITUTE OF BOTANY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c INSTITUTE OF BIOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOLEVULINIC ACID; BINDING PROTEIN; DIMER; GLUTAMIC ACID TRANSFER RNA; GLUTAMIC ACID TRANSFER RNA REDUCTASE; GLUTAMIC ACID TRANSFER RNA REDUCTASE BINDING PROTEIN; HEME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARABIDOPSIS; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; PRIORITY JOURNAL;

ALDEHYDE OXIDOREDUCTASES; AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GLUTAMATES; GLUTAMIC ACID; HEME; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; NADP; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECOMBINANT PROTEINS; RNA-BINDING PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STATIC ELECTRICITY;

EID: 84899807459     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1400166111     Document Type: Article

References (36)

1. Mochizuki N, et al. (2010) The cell biology of tetrapyrroles: A life and death struggle. Trends Plant Sci 15(9):488-498
2. Jahn D, Verkamp E, Söll D (1992) Glutamyl-transfer RNA: A precursor of heme and chlorophyll biosynthesis. Trends Biochem Sci 17(6):215-218
3. Tanaka R, Tanaka A (2007) Tetrapyrrole biosynthesis in higher plants. Annu Rev Plant Biol 58:321-346
4. Czarnecki O, Grimm B (2012) Post-translational control of tetrapyrrole biosynthesis in plants, algae, and cyanobacteria. J Exp Bot 63(4):1675-1687
5. Beale SI (1999) Enzymes of chlorophyll biosynthesis. Photosynth Res 60:43-73
6. Meskauskiene R, et al. (2001) FLU: A negative regulator of chlorophyll biosynthesis in Arabidopsis thaliana. Proc Natl Acad Sci USA 98(22):12826-12831
7. Goslings D, et al. ( 2004) Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1), the target of metabolic feedback inhibition of tetrapyrrole biosynthesis, in dark- and light-grown Arabidopsis plants. Plant J 40(6):957-967
8. Czarnecki O, et al. (2011) An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts. Plant Cell 23(12): 4476-4491
9. Jung HS, et al. (2010) Arabidopsis thaliana PGR7 encodes a conserved chloroplast protein that is necessary for efficient photosynthetic electron transport. PLoS ONE 5(7):e11688
10. Czarnecki O, G rimm B (2013) New insights in the topology of the biosynthesis of 5-aminolevulinic acid. Plant Signal Behav 8(2):e23124
11. Moser J, et al. (2001) V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis. EMBO J 20(23):6583-6590
12. Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN (1997) Crystal structure of glutamat e-1-semialdehyde aminomutase: An 2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity. Proc Natl Acad Sci USA 94(10):4866-4871
13. Moser J, Lorenz S, Hubschwerle n C, Rompf A, Jahn D (1999) Methanopyrus kandleri glutamyl-tRNA reductase. J Biol Chem 274(43):30679-30685
14. Scha uer S, et al. (2002) Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate. J Biol Chem 277(50):48657-48663
15. Schubert WD, Moser J, Schauer S, Heinz DW, Ja hn D (2002) Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes. Photosynth Res 74(2):205-215
16. Lü er C, et al. (2007) Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase. FEBS J 274(17):4609-4614
17. Slesarev AI, et al. (2002) The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens. Proc Natl Acad Sci USA 99(7):4644-4649
18. Lü er C, et al. (2005) Complex formation between glutamyl-tRNA reductase and glutamate- 1-semialdeh yde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis. J Biol Chem 280(19):18568-18572
19. Schulze JO, Schubert WD, Moser J, Jahn D, Heinz DW (2006) Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis. J Mol Biol 358(5):1212-1220
20. Richter AS, Grimm B (2013) Thiol-based redox control of enzymes involved in the tetrapyrrole biosynthesis pathway in plants. Front Plant Sci 4:371
21. Punta M, et al. (2012) The Pfam protein families database. Nucleic Acids Res vol 40(database issue):D290-D301
22. Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW (1998) Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat Struct Biol 5(7):561-567
23. Stetefeld J , Jenny M, Burkhard P (2006) Intersubunit signaling in glutamate-1-semialdehyde- aminomutase. Proc Natl Acad Sci USA 103(37):13688-13693
24. Vothknecht UC, Kannangara CG, von Wettstein D (1996) Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase. Proc Natl Acad Sci USA 93(17):9287-9291
25. Srivast ava A, Beale SI (2005) Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit. J Bacteriol 187(13):4444-4450
26. Nogaj LA, Beale SI (2005) Physical and kinetic interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase of Chlamydomonas reinhardtii. J Biol Chem 280(26):24301-24307
27. Holm L , Kääriäinen S, Rosenström P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24(23):2780-2781
28. Hu Y, et al. (2011) Crystal structure of HugZ, a novel heme oxygenase from Helicobacter pylori. J Biol Chem 286(2):1537-1544
29. Wilks A, Burkhard KA (2007) Heme and virulence: How bacterial pathogens regulate, transport and utilize heme. Nat Prod Rep 24(3):511-522
30. Sekine S, Nureki O, Shimada A, Vassylyev DG, Yokoyama S (2001) Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Nat Struct Biol 8(3):203-206
31. Randau L, et al. (2004) tRNA recognition by glutamyl-tRNA reductase. J Biol Chem 279(33):34931-34937
32. Otwinowski Z, Borek D, Majewski W, Minor W (2003) Multiparametric scaling of diffraction intensities. Acta Crystallogr A 59(pt 3):228-234
33. Ada ms PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(pt 2):213-221
34. Emsley P, Lohkamp B, Scott WG, Cowtan K (2010) Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66(Pt 4):486-501
35. Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26(2):283-291
36. Wiseman T, Williston S, Brandts JF, Lin LN (1989) Rapid measurement of binding constants and heats of binding using a new titra tion calorimeter. Anal Biochem 179(1):131-137