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Bombyx mori , domesticated silkmoth, Pheromone-Binding Protein 1

Bombyx mori , domesticated silkmoth, Pheromone-Binding Protein 1 . Presented by: Tommy W. McGaha Jr. Advanced Biochemistry and Molecular Biology I BCMB 8010 11/30/10. Bombykol. Background of Pheromone-binding proteins.

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Bombyx mori , domesticated silkmoth, Pheromone-Binding Protein 1

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  1. Bombyx mori, domesticated silkmoth, Pheromone-Binding Protein 1 Presented by: Tommy W. McGaha Jr. Advanced Biochemistry and Molecular Biology I BCMB 8010 11/30/10

  2. Bombykol Background of Pheromone-binding proteins • Pheromone-binding proteins (PBPs) are used to transport pheromones, semiochemicals, from the outside environment through the aqueous sensillary lymph to dendritic-odorant receptors. • Bombykol, first discovered sex pheromone, of Bombyx mori (Silk Moth) by Butenandt in 1959 • BmorPBP1 was first isolated by Maida et al. in 1993

  3. First Determined BmorPBP1 Structure via X-ray diffraction (1DQE) Sandler et al. (2000) Chemistry & Biology 7, 142-151 • Expressed from E. coli • Structure determined at pH of 8.2 • Secondary structure • 6 α-helices connected by loops • 3 disulfide bonds: 1) C19-C54, 2) C50-C108, and 3) C97-C117 • Hydrophobic binding pocket • Antiparallel α-helices 1, 4, 5, and 6 • Lid (residues 60-69) • Loop between α-helices 3 and 4 • Closes hydrophobic binding pocket Movie made using eMovie. Hodis, E., Schreiber, G., Rother, K., Sussman, J.L., eMovie: a storyboard-based tool for making molecular movies, Trends in Biochemical Sciences32, 199-204 (2007).Image was created using Pymol version 1.3 with pdb 1DQE from Sandler et al. (2000) Chemistry & Biology 7, 142-151

  4. BmorPBP1 Hydrophobic Pocket Residues with bombykol (1DQE) Bombykol Display of BmorPBP1 hydrophobic pocket was created using Pymol version 1.3 and pdb: 1DQE. 1DQE pdb was produced by: Sandler et al. (2000) Chemistry & Biology 7, 142-151

  5. Hydrophobic pocket “Lid” • “Lid” is the loop region between α-helix 3 and α-helix 4. • Histidine residues: H70 and H95 act as a pH-dependent switch • When protonated, possible interaction with Glu98 and Asp63 • Lid instability in low pH Movie made using eMovie. Hodis, E., Schreiber, G., Rother, K., Sussman, J.L., eMovie: a storyboard-based tool for making molecular movies, Trends in Biochemical Sciences32, 199-204 (2007).  Image was created using Pymol version 1.3 with pdb 1DQE from Sandler et al. (2000) Chemistry & Biology 7, 142-151

  6. Hydrophobic pocket “Lid” BmorPBP1 B-form (1LS8) BmorPBP1 A-form (1GM0) H95 Lid E98 H70 H95 H70 D63 E98 D63 Lid Images of BmorPBP1 Lid was created using Pymol version 1.3 with pdbs 1GM0 and 1LS8. 1GM0 pdb was produced by: Horst et al. (2001) PNAS 98, 14374-14379. 1LS8 pdb was produced by: Lee et al. (2002) FEBS Letters 531, 314-318.

  7. COOH-Terminus Tail Movie made using eMovie. Hodis, E., Schreiber, G., Rother, K., Sussman, J.L., eMovie: a storyboard-based tool for making molecular movies, Trends in Biochemical Sciences32, 199-204 (2007).  Image was created using Pymol version 1.3 with pdb1LS8 from Lee et al. (2002) FEBS Letters 531, 314-318.

  8. COOH-Terminus Tail • C-Terminus Tail (residues: 132-142) • pH dependent residues: Asp132, Glu137, and Glu141 • When protonated form α-helix 7 • α-helix 7 has an high affinity with hydrophobic pocket BmorPBP1 B-Form (1LS8) BmorPBP1 A-form (1GM0) E141 D132 E141 D132 E137 E137 Images of COOH-terminus tail of BmorPBP1 was created using Pymol version 1.3 with pdb: 1LS8 and 1GM0. Pdb 1LS8 was produced by: Lee et al. (2002) FEBS Letters 531, 314-318. Pdb 1GM0 was produced by: Horst et al. (2001) PNAS 98, 14374-14379.

  9. BmorPBP1 (B-form) without ligand (2FJY) Image of B-form BmorPBP1 without ligand and COOH-terminus tail in alpha helical form was created using Pymol version 1.3 and pdb 2FJY from: Lautenschlager, Leal, and Clardy (2005) Biochemical and Biophysical Research Communications 335, 1044-1050

  10. Mechanism BmorPBP1 B-Form (1LS8) BmorPBP1 A-form (1GM0) BmorPBP1 B-Form (2FJY) BmorPBP1 B-Form (1DQE) BmorPBP1 A-form (1GM0) Picture was reproduced with permission from Dr. Walter S. Leal from: Lautenschlager, Leal, and Clardy (2007) Structure 15, 1148-1154. Animation was supplied with displays created by Pymol version 1.3 and pdb sources: 1DQE, 1GM0, 1LS8, and 2FJY

  11. Conclusion • All 4 structures of BmorPBP1 help aid Lautenschlager and colleagues proposed mechanism. • Can knowledge and techniques from these studies help identify an oviposition pheromone-binding protein in black flies? Acknowledgements Special thanks to Dr. Walter S. Leal for supplying animations and pictures to me and giving permission to use them in my presentation. Background picture reproduced with the permission of Dr. Walter S. Leal

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