Catalysis within the lipid bilayer-structure and mechanism of the MAPEG family of integral membrane proteins

Current Opinion in Structural Biology

Volumn 18, Issue 4, 2008, Pages 442-449

  Martinez Molina, Daniel ^a,b   Eshaghi, Said ^a   Nordlund, Pär ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; LEUKOTRIENE C4; MEMBRANE ASSOCIATED PROTEINS IN EICOSANOID AND GLUTATHIONE METABOLISM; MEMBRANE PROTEIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; BINDING SITE; CATALYSIS; ENZYME ACTIVATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; GLUTATHIONE; LIPID BILAYERS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 49549119156     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.04.005     Document Type: Review

References (19)

1. Bresell A., Weinander R., Lundqvist G., Raza H., Shimoji M., Sun T.-H., Balk L., Wiklund R., Eriksson J., Jansson C., et al. Bioinformatic and enzymatic characterization of the MAPEG superfamily. FEBS J 272 (2005) 1688-1703. The authors show an extensive multiple sequence alignment of MAPEG proteins from several species and present an evolutionary division of the members.
2. Hebert H., and Jegerschold C. The structure of membrane associated proteins in eicosanoid and glutathione metabolism as determined by electron crystallography. Curr Opin Struct Biol 17 (2007) 396-404
3. Samuelsson B., Morgenstern R., and Jakobsson P.-J. Membrane prostaglandin E synthase-1: a novel therapeutic target. Pharmacol Rev 59 (2007) 207-224
4. Jakobsson P.-J., Morgernstern R., Mancini J., Ford-Hutchinson A., and Persson B. Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily. Am J Respir Crit Care Med 161 (2000) 20S-24
5. Lam B.K., and Austen K.F. Leukotriene C4 synthase: a pivotal enzyme in cellular biosynthesis of the cysteinyl leukotrienes. Prostaglandins Other Lipid Mediat 68-69 (2002) 511-520
6. Bisgaard H. Leukotriene modifiers in pediatric asthma management. Pediatrics 107 (2001) 381-390. A rich overview on the medical aspects of leukotriene signaling.
7. Byrum R.S., Goulet J.L., Griffiths R.J., and Koller B.H. Role of the 5-lipoxygenase-activating protein (FLAP) in murine acute inflammatory responses. J Exp Med 185 (1997) 1065-1075
8. Johansson K., Ahlen K., Rinaldi R., Sahlander K., Siritantikorn A., and Morgenstern R. Microsomal glutathione transferase 1 in anticancer drug resistance. Carcinogenesis 28 (2007) 465-470
9. Siritantikorn A., Johansson K., Ahlen K., Rinaldi R., Suthiphongchai T., Wilairat P., and Morgenstern R. Protection of cells from oxidative stress by microsomal glutathione transferase 1. Biochem Biophys Res Commun 355 (2007) 592-596
10. Svensson R., Alander J., Armstrong R., and Morgenstern R. Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal glutathione transferase 1. Biochemistry 43 (2004) 8869-8877
11. Holm P.J., Bhakat P., Jegerschold C., Gyobu N., Mitsuoka K., Fujiyoshi Y., Morgenstern R., and Hebert H. Structural basis for detoxification and oxidative stress protection in membranes. J Mol Biol 360 (2006) 934-945. This paper presents the first structure of a MAPEG member, the electron crystallography structure of rat MGST1 at 3.2 Å resolution, and suggests a binding mode for GSH.
12. Schmidt-Krey I., Kanaoka Y., Mills D.J., Irikura D., Haase W., Lam B.K., Austen K.F., and Kuhlbrandt W. Human leukotriene C(4) synthase at 4.5 Å resolution in projection. Structure 12 (2004) 2009-2014
13. Holm P.J., Morgenstern R., and Hebert H. The 3-D structure of microsomal glutathione transferase 1 at 6 Å resolution as determined by electron crystallography of p22121 crystals. Biochim Biophys Acta 1594 (2002) 276-285
14. Martinez Molina D., Wetterholm A., Kohl A., McCarthy A.A., Niegowski D., Ohlson E., Hammarberg T., Eshaghi S., Haeggstrom J.Z., and Nordlund P. Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase 448 (2007) 613-616. The high resolution crystal structure of human LTC4S in complex with GSH and in apo form are described. The molecular basis for aligning the substrates is postulated as well as a reaction scheme.
15. ••]. As a support for the suggested substrate binding mode, they present what they argue to be a S-hexyl-GSH complex at 5.0 Å resolution. This structure, however, has several problems and should be treated with caution.
16. Ferguson A.D., McKeever B.M., Xu S., Wisniewski D., Miller D.K., Yamin T.-T., Spencer R.H., Chu L., Ujjainwalla F., Cunningham B.R., et al. Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science 317 (2007) 510-512. The authors present the low-resolution crystal structure of human FLAP in complex with inhibitors.
17. Busenlehner L., Alander J., Jegerscohld C., Holm P., Bhakat P., Hebert H., Morgenstern R., and Armstrong R. Location of substrate binding sites within the integral membrane protein microsomal glutathione transferase-1. Biochemistry 46 (2007) 2812-2822
18. Chandler D. Interfaces and the driving force of hydrophobic assembly. Nature 437 (2005) 640-647
19. Jakschik B., Sams A., Sprechert H., and Needleman P. Fatty acid structural requirements for leukotriene biosynthesis. Prostaglandins 20 (1980) 401-410