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PDBsum entry 1plp

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Membrane protein PDB id
1plp
Jmol
Contents
Protein chain
25 a.a.
PDB id:
1plp
Name: Membrane protein
Title: Solution structure of the cytoplasmic domain of phospholamban
Structure: Phospholamban. Chain: a. Synonym: plb(1-25). Engineered. Engineered: yes. Mutation: yes. Other_details: nmr, 20 structures
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 20 models
Authors: R.J.Mortishire-Smith,S.M.Pitzenberger,C.J.Burke, C.R.Middaugh,V.M.Garsky,R.G.Johnson
Key ref:
R.J.Mortishire-Smith et al. (1995). Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure. Biochemistry, 34, 7603-7613. PubMed id: 7779806 DOI: 10.1021/bi00023a006
Date:
01-May-95     Release date:   31-Jul-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P26678  (PPLA_HUMAN) -  Cardiac phospholamban
Seq:
Struc:
52 a.a.
25 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     calcium ion transport   1 term 
  Biochemical function     calcium channel regulator activity     2 terms  

 

 
DOI no: 10.1021/bi00023a006 Biochemistry 34:7603-7613 (1995)
PubMed id: 7779806  
 
 
Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure.
R.J.Mortishire-Smith, S.M.Pitzenberger, C.J.Burke, C.R.Middaugh, V.M.Garsky, R.G.Johnson.
 
  ABSTRACT  
 
Peptides representing the N-terminal domain (Ia) of the cardiac sarcoplasmic reticulum protein phospholamban (residues 1-25 [PLB(1-25)] and a phosphorylated form [pPLB(1-25)]) were synthesized and their conformations examined using circular dichroism and nuclear magnetic resonance spectroscopy. In aqueous solution, both PLB(1-25) and pPLB(1-25) adopt a primarily disordered conformation. In 30% trifluoroethanol/10 mM phosphate, PLB(1-25) exhibits a CD spectrum consistent with 60% helical structure. This value decreases to 27% for the phosphorylated peptide. CD spectra in 2% SDS indicate 40% alpha-helix for PLB(1-25) and 20% for pPLB(1-25). Full chemical shift assignments were obtained by conventional homonuclear NMR methodologies for both PLB(1-25) and pPLB(1-25) in 30% trifluoroethanol/water and 300 mM SDS. The solution structure of PLB(1-25) in 30% TFE/water was determined from distance geometry calculations using 54 NOE distance constraints and 17 torsion angle constraints. In the family of 20 calculated conformers, the root mean square deviation from the mean structure is 0.79 A for backbone heavy atoms of residues 1-17. The structure comprises a regular alpha-helix extending from M1 to S16 with the remaining C-terminal residues disordered. The calculated structure is supported by analysis of C alpha H secondary shifts which are significantly negative for residues 1-16. Chemical shift degeneracy is substantially more extensive in the phospho form and precludes a direct comparison of calculated structures. However, the magnitudes of upfield secondary shifts are decreased by 20% in residues 1-11 and are not significantly helical for residues 12-16 according to the criteria of Wishart et al. [(1992) Biochemistry 31, 1647-1651]. 3JHN alpha coupling constants measured for I12, R13, A15, and S16 also suggest that residues 12-16 undergo a local unwinding of the helix upon phosphorylation. Similar results are obtained for PLB(1-25) and pPLB(1-25) in 300 mM perdeuterated sodium dodecyl sulfate except that differences in backbone dynamics for the helical and nonhelical regions of the peptide are evident in the DQF-COSY line shapes for fingerprint cross-peaks. This disruption of structure at the C-terminus of the helix suggests a model for phosphorylation-induced dissociation of the PLB/Ca(2+)-ATPase complex.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19761758 P.Teriete, K.Thai, J.Choi, and F.M.Marassi (2009).
Effects of PKA phosphorylation on the conformation of the Na,K-ATPase regulatory protein FXYD1.
  Biochim Biophys Acta, 1788, 2462-2470.  
17154419 S.Pantano, and E.Carafoli (2007).
The role of phosphorylation on the structure and dynamics of phospholamban: a model from molecular simulations.
  Proteins, 66, 930-940.  
17996192 W.Liu, J.Z.Fei, T.Kawakami, and S.O.Smith (2007).
Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52.
  Biochim Biophys Acta, 1768, 2971-2978.  
16533842 D.L.Stokes, A.J.Pomfret, W.J.Rice, J.P.Glaves, and H.S.Young (2006).
Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals.
  Biophys J, 90, 4213-4223.  
17010801 M.M.DeWitt, H.M.MacLeod, B.Soliven, and E.M.McNally (2006).
Phospholamban R14 deletion results in late-onset, mild, hereditary dilated cardiomyopathy.
  J Am Coll Cardiol, 48, 1396-1398.  
15787961 A.M.Slovic, J.D.Lear, and W.F.DeGrado (2005).
De novo design of a pentameric coiled-coil: decoding the motif for tetramer versus pentamer formation in water-soluble phospholamban.
  J Pept Res, 65, 312-321.  
15501941 C.W.Sikora, and R.J.Turner (2005).
Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry.
  Biophys J, 88, 475-482.  
15764655 M.G.Paterlini, and D.D.Thomas (2005).
The alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation.
  Biophys J, 88, 3243-3251.  
12538897 A.M.Slovic, C.M.Summa, J.D.Lear, and W.F.DeGrado (2003).
Computational design of a water-soluble analog of phospholamban.
  Protein Sci, 12, 337-348.  
12525698 C.Toyoshima, M.Asahi, Y.Sugita, R.Khanna, T.Tsuda, and D.H.MacLennan (2003).
Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.
  Proc Natl Acad Sci U S A, 100, 467-472.  
12838339 D.H.MacLennan, and E.G.Kranias (2003).
Phospholamban: a crucial regulator of cardiac contractility.
  Nat Rev Mol Cell Biol, 4, 566-577.  
12606549 J.Song (2003).
Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties.
  J Biol Chem, 278, 24714-24720.  
12833255 N.A.Lockwood, R.S.Tu, Z.Zhang, M.V.Tirrell, D.D.Thomas, and C.B.Karim (2003).
Structure and function of integral membrane protein domains resolved by peptide-amphiphiles: application to phospholamban.
  Biopolymers, 69, 283-292.  
12080135 P.Pollesello, and A.Annila (2002).
Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.
  Biophys J, 83, 484-490.  
11463632 H.S.Young, L.R.Jones, and D.L.Stokes (2001).
Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy.
  Biophys J, 81, 884-894.  
11526231 M.Asahi, N.M.Green, K.Kurzydlowski, M.Tada, and D.H.MacLennan (2001).
Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases.
  Proc Natl Acad Sci U S A, 98, 10061-10066.  
11371203 Q.Yao, L.T.Chen, J.Li, K.Brungardt, T.C.Squier, and D.J.Bigelow (2001).
Oligomeric interactions between phospholamban molecules regulate Ca-ATPase activity in functionally reconstituted membranes.
  Biochemistry, 40, 6406-6413.  
11488924 S.W.Vetter, and E.Leclerc (2001).
Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.
  Eur J Biochem, 268, 4292-4299.  
10809745 M.Asahi, E.McKenna, K.Kurzydlowski, M.Tada, and D.H.MacLennan (2000).
Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP.
  J Biol Chem, 275, 15034-15038.  
9876124 A.Tholey, A.Lindemann, V.Kinzel, and J.Reed (1999).
Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance study.
  Biophys J, 76, 76-87.  
10551848 M.Asahi, Y.Kimura, K.Kurzydlowski, M.Tada, and D.H.MacLennan (1999).
Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites.
  J Biol Chem, 274, 32855-32862.  
10096878 P.Pollesello, A.Annila, and M.Ovaska (1999).
Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer.
  Biophys J, 76, 1784-1795.  
10603934 D.H.MacLennan, Y.Kimura, and T.Toyofuku (1998).
Sites of regulatory interaction between calcium ATPases and phospholamban.
  Ann N Y Acad Sci, 853, 31-42.  
9601048 M.Li, R.L.Cornea, J.M.Autry, L.R.Jones, and D.D.Thomas (1998).
Phosphorylation-induced structural change in phospholamban and its mutants, detected by intrinsic fluorescence.
  Biochemistry, 37, 7869-7877.  
10603985 R.G.Johnson (1998).
Pharmacology of the cardiac sarcoplasmic reticulum calcium ATPase-phospholamban interaction.
  Ann N Y Acad Sci, 853, 380-392.  
10603937 R.J.Mortishire-Smith, H.Broughton, V.M.Garsky, E.J.Mayer, and R.G.Johnson (1998).
Structural studies on phospholamban and implications for regulation of the Ca(2+)-ATPase.
  Ann N Y Acad Sci, 853, 63-78.  
9603928 Y.Kimura, M.Asahi, K.Kurzydlowski, M.Tada, and D.H.MacLennan (1998).
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum.
  J Biol Chem, 273, 14238-14241.  
9209158 A.Borroto, M.A.Jiménez, B.Alarcón, and M.Rico (1997).
1H-NMR analysis of CD3-epsilon reveals the presence of turn-helix structures around the ITAM motif in an otherwise random coil cytoplasmic tail.
  Biopolymers, 42, 75-88.  
9218476 A.Nilsson, D.Stys, T.Drakenberg, M.D.Spangfort, S.Forsén, and J.F.Allen (1997).
Phosphorylation controls the three-dimensional structure of plant light harvesting complex II.
  J Biol Chem, 272, 18350-18357.  
9266178 D.L.Stokes (1997).
Keeping calcium in its place: Ca(2+)-ATPase and phospholamban.
  Curr Opin Struct Biol, 7, 550-556.  
9370444 F.A.Kovacs, and T.A.Cross (1997).
Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation.
  Biophys J, 73, 2511-2517.  
9202842 P.Karczewski, M.Kuschel, L.G.Baltas, S.Bartel, and E.G.Krause (1997).
Site-specific phosphorylation of a phospholamban peptide by cyclic nucleotide- and Ca2+/calmodulin-dependent protein kinases of cardiac sarcoplasmic reticulum.
  Basic Res Cardiol, 92, 37-43.  
8702967 Y.Kimura, K.Kurzydlowski, M.Tada, and D.H.MacLennan (1996).
Phospholamban regulates the Ca2+-ATPase through intramembrane interactions.
  J Biol Chem, 271, 21726-21731.  
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.