Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima

FEBS Journal

Volumn 274, Issue 10, 2007, Pages 2461-2469

  Stieglitz, Kimberly A ^b   Roberts, Mary F ^b   Li, Weizhong ^a   Stec, Boguslaw ^a  

^a BURNHAM INSTITUTE   (United States)

^b BOSTON COLLEGE   (United States)

Author keywords

Fructose 1, 6 bisphosphatase; Inositol monophosphatase; Protein folding; Thermophile; Thermotoga maritima

Indexed keywords

BACTERIAL ENZYME; FRUCTOSE BISPHOSPHATASE; INOSITOL 1 PHOSPHATASE; TETRAMER;

ALPHA HELIX; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBUNIT; HYPERTHERMOPHILIC BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; THERMOTOGA MARITIMA;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; EVOLUTION, MOLECULAR; FRUCTOSE-BISPHOSPHATASE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ALIGNMENT; THERMOTOGA MARITIMA;

ARCHAEA; THERMOTOGA MARITIMA;

EID: 34247605062     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.0014-2956.2007.05779.x     Document Type: Article

References (27)

1. Zhang Y, Liang JY Lipscomb WN (1993) Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase. Biochem Biophys Res Commun 190, 1080 1083.
2. York JD, Ponder JW Majerus PW (1995) Definition of a metal-dependent/ Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc Natl Acad Sci USA 92, 5149 5153.
3. Chen L Roberts MF (2000) Overexpression, purification and analysis of complementation behavior of E. coli SuhB protein: Comparison with bacterial and archaeal inositol monophosphatases. Biochemistry 39, 4145 4153.
4. Nimmo HG Tipton KF (1975) The allosteric properties of beef-liver fructose bisphosphatase. Eur J Biochem 58, 575 585.
5. Villeret V, Huang S, Zhang Y, Xue Y Lipscomb WN (1995) Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 Å resolution. Biochemistry 34, 4299 4306.
6. Chen L Roberts MF (1999) Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima. Appl Environ Microbiol 65, 4559 4567.
7. Stec B, Yang H, Johnson KA, Chen L Roberts MF (2000) MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol 7, 1046 1050.
8. Johnson KA, Chen L, Yang H, Roberts MF Stec B (2001) Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities. Biochemistry 40, 618 630.
9. Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF Stec B (2002) Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem 277, 22863 22874.
10. Choe JY, Fromm HJ Honzatko RB (2000) Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes. Biochemistry 39, 8565 8574.
11. Hallcher LM Sherman WR (1980) The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J Biol Chem 255, 10896 10901.
12. Bone R, Springer JP Atack JR (1992) Structure of inositol monophosphatase, the putative target of lithium therapy. Proc Natl Acad Sci USA 89, 10031 10035.
13. Patel S, Yenush L, Rodriguez PL, Serrano R Blundell TL (2002) Crystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3′-phosphoadenosine-5′-phosphate phosphatase activities: a novel target of lithium therapy. J Mol Biol 315, 677 685.
14. Fieve RR (1999) Lithium therapy at the millennium: a revolutionary drug used for 50 years faces competing options and possible demise. Bipolar Disord 1, 67 70.
15. Dunker AK, Brown CJ, Lawson JD, Iakoucheva LM Obradovic Z (2002) Intrinsic disordered and protein function. Biochemistry 41, 6573 6582.
16. Dyson HJ Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6, 197 208.
17. Vagin A Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Cryst 30, 1022 1025.
18. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54, 905 921.
19. Laskowski RA, MacArthur MW, Moss DS Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26, 283 291.
20. Lu G, Stec B, Giroux EL Kantrowitz ER (1996) Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity. Protein Sci 5, 2333 2342.
21. Zhang Y, Liang J-Y, Huang S Lipscomb WN (1994) Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. J Mol Biol 244, 609 624.
22. Dunker AK, Lawson JD, Brown CJ, Williams RM, Romero P, Oh JS, Oldfield CJ, Campen AM, Ratliff CM, Hipps KW et al. (2001) Intrinsically disordered protein. J Mol Graph Model 19, 26 59.
23. Siebert X Amzel LM (2004) Loss of translational entropy in molecular associations. Proteins: Struct Funct Genet 54, 104 115.
24. Li W, Jaroszewski L Godzik A (2001) Clustering of highly homologous sequences to reduce the size of large protein databases. Bioinformatics 17, 282 283.
25. Thompson JD, Higgins DG Gibson TJ (1994) clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673 4680.
26. Kabsch W Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577 2637.
27. Li W Godzik A (2006) VISSA: a program to visualize structural features from structure sequence alignment. Bioinformatics 22, 887 888.