Structural comparison of oxidized and reduced FKBP13 from Arabidopsis thaliana

Proteins: Structure, Function and Genetics

Volumn 65, Issue 4, 2006, Pages 789-795

  Gopalan, Gayathri ^a,e   He, Zengyong ^b   Battaile, Kevin P ^c   Luan, Sheng ^b   Swaminathan, Kunchithapadam ^a,d  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c ARGONNE NATIONAL LABORATORY   (United States)

^d INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^e ARIZONA STATE UNIVERSITY   (United States)

Author keywords

Dithiothreitol; PPIase; Redox regulation; Reduced disulfide bonds; X ray crystal structure

Indexed keywords

AMINO ACID; CYCLOPHILIN; CYSTEINE; DISULFIDE; DITHIOTHREITOL; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 13; HYDROGEN; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARABIDOPSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHLOROPLAST; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ACTIVITY; HYDROGEN BOND; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; THYLAKOID; X RAY CRYSTALLOGRAPHY;

ARABIDOPSIS PROTEINS; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; TACROLIMUS BINDING PROTEINS;

ARABIDOPSIS THALIANA;

EID: 33751082083     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21108     Document Type: Article

References (39)

1. Schreiber SL. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 1991;251:283-287.
2. He Z, Li L, Luan S. Immunophilins and parvulins: superfamily of peptidyl prolyl isomerases in Arabidopsis. Plant Physiol 2004;134:1248-1267.
3. Romano P, Gray J, Horton P, Luan S. Plant immunophilins: functional versatility beyond protein maturation. New Phytol 2005;66:753-769.
4. Berardini TZ, Bollman K, Sun H, Poethig RS. Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40. Science 2001;291:2405-2407.
5. Luan S, Albers MW, Schreiber SL. Light-regulated, tissue-specific immunophilins in a higher plant. Proc Natl Acad Sci USA 1994;91:984-988.
6. Luan S, Lane WS, Schreiber SL. pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from fava bean. Plant Cell 1994;6:885-892.
7. Lippuner V, Chou IT, Scott SV, Ettinger WF, Theg SM, Gasser CS. Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana. J Biol Chem 1994;269:7863-7868.
8. Schubert M, Petersson UA, Haas BJ, Funk C, Schroder WP, Kieselbach T. Proteome map of the chloroplast lumen of Arabidopsis thaliana. J Biol Chem 2002;277:8354-8365;
9. Erratum J Biol Chem 2003;278:13590.
10. Gupta R, Mould RM, He Z, Luan S. A chloroplast FKBP interacts with and affects the accumulation of Rieske subunit of cytochrome bf complex. Proc Natl Acad Sci USA 2002;99:15806-15811.
11. Peltier JB, Emanuelsson O, Kalume DE, Ytterberg J, Friso G, Rudella A, Liberles DA, Soderberg L, Roepstorff P, von Heijne G, van Wijk KJ. Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction. Plant Cell 2002;14:21123-21126.
12. Romano P, He Z, Luan S. Introducing immunophilins: from organ transplantation to plant biology. Plant Physiol 2004;134:1241-1243.
13. Gopalan G, He Z, Balmer Y, Romano P, Gupta R, Heroux A, Buchanan BB, Swaminathan K, Luan S. Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen. Proc Natl Acad Sci USA 2004;101:13945-13950.
14. Buchanan BB, Luan S. Redox regulation in the chloroplast thylakoid lumen: a new frontier in photosynthesis research. J Exp Bot 2005;56:1439-1447.
15. Qin J, Clore GM, Gronenborn AM. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 1994;2:503-522.
16. Jeng M-F, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ. High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 1994;2:853-868.
17. Hirotsu S, Abe Y, Okada K, Nagahara N, Hori H, Nishino T, Hakoshima T. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc Natl Acad Sci USA 1999;96:12333-12338.
18. Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 1996;35:7684-7691.
19. McCarthy AA, Haebel PW, Törrönen A, Rybin V, Baker EN, Metcalf P. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat Struct Biol 2000;7:196-199.
20. Rozhkova A, Stirnimann CU, Frei P, Grauschopf U, Brunisholz R, Grütter MG, Capitani G, Glockshuber R. Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. EMBO J 2004;23:1709-1719.
21. Creighton TE. Disulfide bonds as probes of protein folding pathways. Methods Enzymol 1986;131:83-106.
22. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
23. Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
24. Vagin A, Taplyakov A. MOLREP - an automated program for molecular replacement. J Appl Crystallogr 1997;30:1022-1025.
25. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
26. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography & NMR System: A new software system for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998;54:905-921.
27. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK - a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
28. Hooft RWW, Vriend G, Sander C, Abola EE. Errors in protein structures. Nature 1996;381:272.
29. Kraulis PJ. Molscript - a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
30. Merritt EA, Bacon DJ. Raster3D-photorealistic molecular graphics. Methods Enzymol 1997;277:505-524.
31. Banaszak K, Mechin I, Frost G, Rypniewski W Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli. Acta Crystallogr D Biol Crystallogr 2004;60:1747-1752.
32. Becker JW, Rotonda J, McKeever BM, Chan HK, Marcy AI, Wiederrecht G, Hermes JD, Springer JP. FK-506-binding protein: three-dimensional structure of the complex with the antagonist L-685,818. J Biol Chem 1993;268:11335-11339.
33. Yang D, Rosen MK, Schreiber SL. A composite FKBP12-FK506 surface that contacts calcineurin. J Am Chem Soc 1993;115:819-820.
34. Sowddhamini R, Srinivasan N, Shoichet B, Santi DV, Ramakrishnan C, Balaram P. Stereochemical modeling of disulfide bridges: criteria for introduction into proteins by site-directed mutagenesis. Protein Eng 1989;3:95-103.
35. Mössner E, Huber-Wunderlich M, Glockshuber R. Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases. Protein Sci 1998;7:1233-1244.
36. Weichsel A, Gasdaska JR, Powis G, Montfort WR. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 1996;4:735-751.
37. Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM. High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry 1991;30:2685-2698.
38. Villeret V, Huang S, Zhang Y, Xue Y, Lipscomb WN. Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 Å resolution. Biochemistry 1995;34:4299-4306.
39. Carr PD, Verger D, Ashton AR, Ollis DL. Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Struct Fold Des 1999;7:461-475.