Bacteriorhodopsin
From Proteopedia
Revision as of 18:41, 27 September 2017 by Michal Harel (talk | contribs)
FunctionBacteriorhodopsin (Br) is a membrane protein in Archaea which moves protons across the cell membrane. See also Bacteriorhodopsin (Hebrew). Structural highlightsBr is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. The retinal interacts predominantly with hydrophobic and aromatic residues [1] (Hydrophobic, Polar).
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3D Structures of bacteriorhodopsin
Updated on 27-September-2017
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- Bacteriorhodopsin
- Bacteriorhodopsin (Hebrew), 3nsb, 3mbv, 1x0s, 1x0i, 1x0k, 1xji, 1iw6, 4fpd, 2i1x, 1kme, 1qm8, 1bm1, 1brr, 2brd, 4hyx, 4xxj, 4y9h, 5a44, 5a45, 5b34, 5b35, 5b6v, 5b6w, 5b6x, 5b6y, 5b6z, 5h2h, 5h2i, 5h2j, 5h2k, 5h2l, 5h2m– HsBr residues 14-261 + lipid + retinal – Halobacterium salinarum
- 3vhz - HsBr (mutant) + lipid + retinal
- 2wjk, 2wjl - HsBr residues 14-261 (mutant) + lipid + retinal
- 3han, 2hao, 3hap, 3haq, 3har, 3has, 3coc, 3cod, 1tn5, 1tn0, 1s51, 1s52, 1s53, 1s54, 1q5i, 1q5j, 1pxr, 1pxs, 3hao, 3utv, 3utw, 3utx, 3uty - HsBr residues 14-261 (mutant) + retinal
- 2ntu, 1py6, 1fbb, 1fbk, 1brx, 1ap9, 1at9, 5br2, 5br5 - HsBr residues 14-261 + retinal
- 4x31, 4x32 - HsBr residues 14-261 + lipid + retinal
- 2at9 - HsBr residues 14-261 + lipid + retinal – Cryo EM
- 1brd - HsBr residues 14-261 + retinal – Cryo EM
- 1s8j, 3t45 - HsBr residues 14-261 (mutant) + lipid + NO3 + retinal
- 1mgy - HsBr residues 14-261 (mutant) + lipid + Br + retinal
- 1s8l - HsBr residues 14-261 (mutant) + lipid + retinal
- 4md1, 4md2, 4ov0 - HsBr residues 14-261 + lipid
- 1qhj - HsBr residues 14-261 + phytanyl derivavative + retinal
- 4hwl – HsBr + heptane + hexane + retinal
- 1r84, 1r2n - HsBr residues 1-232 + retinal – NMR
- 1bct - HsBr residues 163-231 – NMR
- 1bha, 1bhb - HsBr residues 1-71 - NMR
- 1l0m – Br (mutant) – Halobacterium halobium - NMR
- 4pxk - Br (mutant) – Haloarcula marismortuim
- 4qi1, 4qid – HwBr-I – Haloquadratum walsbyi
- 4wav – HwBr-I (mutant)
- 5azd – Br – Thermus thermophilus
- Bacteriorhodopsin (Hebrew), 3nsb, 3mbv, 1x0s, 1x0i, 1x0k, 1xji, 1iw6, 4fpd, 2i1x, 1kme, 1qm8, 1bm1, 1brr, 2brd, 4hyx, 4xxj, 4y9h, 5a44, 5a45, 5b34, 5b35, 5b6v, 5b6w, 5b6x, 5b6y, 5b6z, 5h2h, 5h2i, 5h2j, 5h2k, 5h2l, 5h2m– HsBr residues 14-261 + lipid + retinal – Halobacterium salinarum
- Bacteriorhodopsin intermediates
- 1f50, 1c8r - HsBr-BR residues 18-244 (mutant) + lipid + retinal
- 1c3w - HsBr-BR residues 5-231 + lipid + retinal
- 2zfe – HsBr-K residues 14-261 + lipid + retinal
- 1m0k, 1m0l, 1ixf - HsBr-K residues 1-261 + lipid + retinal
- 1m0m - HsBr-M1 residues 1-261 + lipid + retinal
- 1e0p, 2ntw, 1vjm - HsBr-L residues 18-245 + retinal
- 1ucq, 1iw9, 1o0a – HsBr-L residues 14-261 + lipid + retinal
- 1kg8, 1kg9, 1kgb, 1dze, 1cwq, 2zzl, 2i20, 2i21, 1p8h - HsBr-M residues 13-243 + lipid + retinal
- 1f4z, 1c8s, 1p8i - HsBr-M residues 18-244 (mutant) + lipid + retinal
- 1p8u – HsBr-N residues 14-261 (mutant) + lipid + retinal
- 1jv6, 1jv7, 3vi0 - HsBr-O residues 1-261 (mutant) + lipid + retinal
- 1qko, 1qkp - HsBr residues 14-261 + retinal
- 1f50, 1c8r - HsBr-BR residues 18-244 (mutant) + lipid + retinal
- Halorhodopsin
- Sensory rhodopsin II
- 2ksy – NpBr – NMR
- 2f93, 2f95, 1h2s - BpBr + Br transducer + detergent + retinal
- 3qap, 3qdc - NpBr + eicosane + lipid + retinal
- 4gyc - NpBr + retinal + eicosane + lipid + Br transducer
- 1gu8, 1gue, 1h68, 1jgj - NpBr + retinal
- 1xio - AnBr + detergent + retinal - Anabaena
- 4tl3 - AnBr (mutant) + detergent + retinal
- 2m3g - AnBr + detergent - NMR
- 2ksy – NpBr – NMR
- Xanthorhodopsin
- 3ddl – Br + detergent + salinixanthin + retinal – Salinibacter ruber
- Archaerhodopsin
- Proteorhodopsin
- Deltarhodopsin
- 4fbz - Rn + bacterioruberin + retinal – Haloterrigena thermotolerans
- 4fbz - Rn + bacterioruberin + retinal – Haloterrigena thermotolerans
See Also
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Wayne Decatur, Jaime Prilusky, Joel L. Sussman