PDBsum entry 1mgy

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Proton transport PDB id
Protein chain
216 a.a. *
LI1 ×8
_BR ×2
Waters ×49
* Residue conservation analysis
PDB id:
Name: Proton transport
Title: Structure of the d85s mutant of bacteriorhodopsin with bromide bound
Structure: Bacteriorhodopsin. Chain: a. Synonym: br. Engineered: yes. Mutation: yes
Source: Halobacterium salinarum. Organism_taxid: 2242. Expressed in: halobacterium salinarum. Expression_system_taxid: 2242
2.00Å     R-factor:   0.215     R-free:   0.236
Authors: M.T.Facciotti,V.S.Cheung,D.Nguyen,S.Rouhani,R.M.Glaeser
Key ref: M.T.Facciotti et al. (2003). Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping. Biophys J, 85, 451-458. PubMed id: 12829500
16-Aug-02     Release date:   07-Jul-03    
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Protein chain
Pfam   ArchSchema ?
P02945  (BACR_HALSA) -  Bacteriorhodopsin
262 a.a.
216 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   3 terms 
  Biological process     response to stimulus   7 terms 
  Biochemical function     photoreceptor activity     2 terms  


Biophys J 85:451-458 (2003)
PubMed id: 12829500  
Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping.
M.T.Facciotti, V.S.Cheung, D.Nguyen, S.Rouhani, R.M.Glaeser.
We report the crystal structure of a bromide-bound form of the D85S mutant of bacteriorhodopsin, bR(D85S), a protein that uses light energy rather than ATP to pump halide ions across the cell membrane. Comparison of the structure of the halide-bound and halide-free states reveals that both displacements of individual side-chain positions and concerted helical movements occur on the extracellular side of the protein. Analysis of these structural changes reveals how this ion pump first facilitates ion uptake deep within the cell membrane and then prevents the backward escape of ions later in the pumping cycle. Together with the information provided by structures of intermediate states in the bacteriorhodopsin photocycle, this study also suggests the overall design principles that are necessary for ion pumping.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20382993 J.M.Holton, and K.A.Frankel (2010).
The minimum crystal size needed for a complete diffraction data set.
  Acta Crystallogr D Biol Crystallogr, 66, 393-408.  
19240325 J.M.Holton (2009).
A beginner's guide to radiation damage.
  J Synchrotron Radiat, 16, 133-142.  
19267875 M.Kubo, T.Kikukawa, S.Miyauchi, A.Seki, M.Kamiya, T.Aizawa, K.Kawano, N.Kamo, and M.Demura (2009).
Role of Arg123 in Light-driven Anion Pump Mechanisms of pharaonis Halorhodopsin.
  Photochem Photobiol, 85, 547-555.  
16731567 R.Efremov, V.I.Gordeliy, J.Heberle, and G.Büldt (2006).
Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics.
  Biophys J, 91, 1441-1451.  
15837200 A.D.Gruia, A.N.Bondar, J.C.Smith, and S.Fischer (2005).
Mechanism of a molecular valve in the halorhodopsin chloride pump.
  Structure, 13, 617-627.  
15240452 H.Jang, P.S.Crozier, M.J.Stevens, and T.B.Woolf (2004).
How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation.
  Biophys J, 87, 129-145.  
15362229 M.T.Facciotti, S.Rouhani-Manshadi, and R.M.Glaeser (2004).
Energy transduction in transmembrane ion pumps.
  Trends Biochem Sci, 29, 445-451.  
15520287 N.S.Baliga, R.Bonneau, M.T.Facciotti, M.Pan, G.Glusman, E.W.Deutsch, P.Shannon, Y.Chiu, R.S.Weng, R.R.Gan, P.Hung, S.V.Date, E.Marcotte, L.Hood, and W.V.Ng (2004).
Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.
  Genome Res, 14, 2221-2234.  
14990493 Z.Bálint, M.Lakatos, C.Ganea, J.K.Lanyi, and G.Váró (2004).
The nitrate transporting photochemical reaction cycle of the pharaonis halorhodopsin.
  Biophys J, 86, 1655-1663.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.