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PDBsum entry 1jh0

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protein ligands metals Protein-protein interface(s) links
Photosynthesis PDB id
1jh0
Jmol
Contents
Protein chains
280 a.a. *
301 a.a. *
238 a.a. *
Ligands
BCL ×4
BPH ×2
U10
SPO
Metals
_FE
Waters ×96
* Residue conservation analysis
PDB id:
1jh0
Name: Photosynthesis
Title: Photosynthetic reaction center mutant with glu l 205 replace
Structure: Photosynthetic reaction center l subunit. Chain: l. Synonym: reaction center protein l chain. Engineered: yes. Mutation: yes. Photosynthetic reaction center m subunit. Chain: m. Synonym: reaction center protein m chain. Engineered: yes.
Source: Rhodobacter sphaeroides. Organism_taxid: 1063. Expressed in: rhodobacter sphaeroides 2.4.1. Expression_system_taxid: 272943.
Biol. unit: Trimer (from PQS)
Resolution:
3.50Å     R-factor:   0.225     R-free:   0.269
Authors: A.Camara-Artigas,C.L.Magee,J.C.Williams,J.P.Allen
Key ref:
A.Camara-Artigas et al. (2001). Individual interactions influence the crystalline order for membrane proteins. Acta Crystallogr D Biol Crystallogr, 57, 1281-1286. PubMed id: 11526320 DOI: 10.1107/S090744490101109X
Date:
27-Jun-01     Release date:   05-Sep-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0C0Y8  (RCEL_RHOSH) -  Reaction center protein L chain
Seq:
Struc:
282 a.a.
280 a.a.*
Protein chain
Pfam   ArchSchema ?
P0C0Y9  (RCEM_RHOSH) -  Reaction center protein M chain
Seq:
Struc:
308 a.a.
301 a.a.
Protein chain
Pfam   ArchSchema ?
P0C0Y7  (RCEH_RHOSH) -  Reaction center protein H chain
Seq:
Struc:
260 a.a.
238 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   4 terms 
  Biological process     oxidation-reduction process   5 terms 
  Biochemical function     electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity     4 terms  

 

 
DOI no: 10.1107/S090744490101109X Acta Crystallogr D Biol Crystallogr 57:1281-1286 (2001)
PubMed id: 11526320  
 
 
Individual interactions influence the crystalline order for membrane proteins.
A.Camara-Artigas, C.L.Magee, J.C.Williams, J.P.Allen.
 
  ABSTRACT  
 
The role of contact interactions in the crystallization of membrane proteins was assessed by mutation of amino-acid residues on the surface of the reaction center from Rhodobacter sphaeroides. Five single-site mutants were constructed, with changes in contact regions found in the trigonal and tetragonal forms but not the orthorhombic form. Crystallization trials for the tetragonal form yielded either no crystals or crystals with an altered morphology, whereas crystals grew in the other two forms, indicating that these interactions are essential for the stability of the tetragonal crystals. Changes in the structures determined by X-ray diffraction of trigonal crystals for each mutant were related to the quality of the diffraction. Significant differences in the resolution limit of the crystals were associated with the loss of specific interactions between neighboring proteins. The results suggest that the contact regions are crucial for obtaining highly ordered crystals of membrane proteins.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Structure of the wild-type reaction center from R. sphaeroides. (a) Backbone with the residues that have been found in a contact site in any one of the three crystal forms. All of the residues are located in the hydrophilic regions away from the central membrane-spanning region. The three residues at which mutations were made are labeled. (b) One of the contact interactions that is found only in the tetragonal form. Shown are residues GluL205 of one protein (shaded with atom types colored) and TyrM76 and LysM110 of a neighboring protein (shaded light tan). The residues form a bridge and hydrogen bonds that probably contribute to the high degree of crystalline order of this form.
Figure 4.
Figure 4 Stereo diagram of a contact region for the trigonal form in the wild type (blue) and the EL(L205) mutant (red). In the wild type, GluL205 interacts with HisH68, which is part of a loop formed by residues H68-H74 that is close to the same loop of a symmetry-related protein. This contact interaction is mediated by water molecules (blue) associated with ThrH72 and ThrH74. The substitution of Leu for Glu at L205 results in the association of a molecule, probably an ion (red), near L205 and H68 and loss of the bridging water molecules.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 1281-1286) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  16511237 D.M.Anstrom, L.Colip, B.Moshofsky, E.Hatcher, and S.J.Remington (2005).
Systematic replacement of lysine with glutamine and alanine in Escherichia coli malate synthase G: effect on crystallization.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 1069-1074.  
  16511142 G.Uyeda, A.Cámara-Artigas, J.C.Williams, and J.P.Allen (2005).
New tetragonal form of reaction centers from Rhodobacter sphaeroides and the involvement of a manganese ion at a crystal contact point.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 733-736.  
15908429 J.A.Potter, P.K.Fyfe, D.Frolov, M.C.Wakeham, R.van Grondelle, B.Robert, and M.R.Jones (2005).
Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center.
  J Biol Chem, 280, 27155-27164.
PDB code: 2boz
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