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PDBsum entry 1quj
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protein ligands metals links
Phosphate transport PDB id
1quj

 

 

 

 

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Contents
Protein chain
321 a.a. *
Ligands
PO4
Metals
_CL
Waters ×189
* Residue conservation analysis
PDB id:
1quj
Name: Phosphate transport
Title: Phosphate-binding protein mutant with asp 137 replaced by gly complex with chlorine and phosphate
Structure: Phosphate-binding protein. Chain: a. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: pan92
Resolution:
1.90Å     R-factor:   0.190     R-free:   0.209
Authors: N.Yao,A.Choudhary,P.S.Ledvina,F.A.Quiocho
Key ref:
N.Yao et al. (1996). Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor. Biochemistry, 35, 2079-2085. PubMed id: 8652549 DOI: 10.1021/bi952686r
Date:
11-Nov-95     Release date:   11-Jul-96    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0AG82  (PSTS_ECOLI) -  Phosphate-binding protein PstS from Escherichia coli (strain K12)
Seq:
Struc: 		346 a.a.
321 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1021/bi952686r Biochemistry 35:2079-2085 (1996)
PubMed id: 8652549  
 
 
Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.
N.Yao, P.S.Ledvina, A.Choudhary, F.A.Quiocho.
 
  ABSTRACT  
 
Electrostatic interactions are among the key forces determining the structure and function of proteins. These are exemplified in the liganded form of the receptor, a phosphate binding protein from Escherichia coli. The phosphate, completely dehydrated and buried in the receptor, is bound by 12 hydrogen bonds as well as a salt link with Arg 135. We have modulated the ionic attraction while preserving the hydrogen bonds by mutating Asp 137, also salt linked to Arg 135, to Asn, Gly or Thr. High-resolution crystallographic analysis revealed that Gly and Thr (but not Asn) mutant proteins have incorporated a more electronegative Cl- in place of the Asp carboxylate. That no dramatic effect on phosphate affinity was produced by these ionic perturbations indicates a major role for hydrogen bonds and other local dipoles in the binding and charge stabilization of ionic ligands.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21205904 J.Liu, L.Qin, and S.Ferguson-Miller (2011).
Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump.
  Proc Natl Acad Sci U S A, 108, 1284-1289.
PDB codes: 3om3 3oma 3omi 3omn
19290474 A.Berna, F.Bernier, E.Chabrière, M.Elias, K.Scott, and A.Suh (2009).
For whom the bell tolls? DING proteins in health and disease.
  Cell Mol Life Sci, 66, 2205-2218.  
19169467 S.Kubik (2009).
Amino acid containing anion receptors.
  Chem Soc Rev, 38, 585-605.  
19019243 M.J.Cuneo, L.S.Beese, and H.W.Hellinga (2008).
Ligand-induced conformational changes in a thermophilic ribose-binding protein.
  BMC Struct Biol, 8, 50.
PDB codes: 2fn8 2fn9
18599641 V.A.Streltsov, S.J.Titmuss, V.C.Epa, K.J.Barnham, C.L.Masters, and J.N.Varghese (2008).
The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease.
  Biophys J, 95, 3447-3456.  
16531243 R.Morales, A.Berna, P.Carpentier, C.Contreras-Martel, F.Renault, M.Nicodeme, M.L.Chesne-Seck, F.Bernier, J.Dupuy, C.Schaeffer, H.Diemer, A.Van-Dorsselaer, J.C.Fontecilla-Camps, P.Masson, D.Rochu, and E.Chabriere (2006).
Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein.
  Structure, 14, 601-609.
PDB code: 2cap
15281134 D.B.Sherman, S.Zhang, J.B.Pitner, and A.Tropsha (2004).
Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.
  Proteins, 56, 828-838.  
12842040 N.K.Vyas, M.N.Vyas, and F.A.Quiocho (2003).
Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions.
  Structure, 11, 765-774.
PDB code: 1pc3
11807752 H.C.Huang, and J.M.Briggs (2002).
The association between a negatively charged ligand and the electronegative binding pocket of its receptor.
  Biopolymers, 63, 247-260.  
10692303 M.R.Gunner, M.A.Saleh, E.Cross, A.ud-Doula, and M.Wise (2000).
Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect.
  Biophys J, 78, 1126-1144.  
9671506 M.Hirshberg, K.Henrick, L.L.Haire, N.Vasisht, M.Brune, J.E.Corrie, and M.R.Webb (1998).
Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.
  Biochemistry, 37, 10381-10385.
PDB codes: 1a54 1a55
  9865949 P.S.Ledvina, A.L.Tsai, Z.Wang, E.Koehl, and F.A.Quiocho (1998).
Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.
  Protein Sci, 7, 2550-2559.
PDB code: 1a40
  9865945 U.Hars, R.Horlacher, W.Boos, W.Welte, and K.Diederichs (1998).
Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose.
  Protein Sci, 7, 2511-2521.
PDB codes: 1byk 4xxh
9309217 F.A.Quiocho, J.C.Spurlino, and L.E.Rodseth (1997).
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.
  Structure, 5, 997.
PDB codes: 1anf 3mbp 4mbp
8994593 K.D.Collins (1997).
Charge density-dependent strength of hydration and biological structure.
  Biophys J, 72, 65-76.  
  9098050 Y.Qi, Y.Kobayashi, and F.M.Hulett (1997).
The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the pho regulon.
  J Bacteriol, 179, 2534-2539.  
9228942 Z.Wang, H.Luecke, N.Yao, and F.A.Quiocho (1997).
A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.
  Nat Struct Biol, 4, 519-522.
PDB codes: 1ixg 1ixh 1ixi
8718866 A.Phelps, C.Briggs, L.Mincone, and H.Wohlrab (1996).
Mitochondrial phosphate transport protein. replacements of glutamic, aspartic, and histidine residues affect transport and protein conformation and point to a coupled proton transport path.
  Biochemistry, 35, 10757-10762.  
8861200 F.A.Quiocho, and P.S.Ledvina (1996).
Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes.
  Mol Microbiol, 20, 17-25.  
8692896 P.S.Ledvina, N.Yao, A.Choudhary, and F.A.Quiocho (1996).
Negative electrostatic surface potential of protein sites specific for anionic ligands.
  Proc Natl Acad Sci U S A, 93, 6786-6791.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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