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PDBsum entry 1n42

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protein ligands metals links
Lipid binding protein PDB id
1n42
Jmol
Contents
Protein chain
318 a.a. *
Ligands
SO4 ×3
Metals
_CA ×5
Waters ×140
* Residue conservation analysis
PDB id:
1n42
Name: Lipid binding protein
Title: Crystal structure of annexin v r149e mutant
Structure: Annexin v. Chain: a. Synonym: lipocortin-v. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Trimer (from PQS)
Resolution:
2.10Å     R-factor:   0.193     R-free:   0.239
Authors: Y.D.Mo,B.Campos,T.R.Mealy,L.Commodore,J.F.Head,J.R.Dedman, B.A.Seaton
Key ref:
Y.Mo et al. (2003). Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces. J Biol Chem, 278, 2437-2443. PubMed id: 12401794 DOI: 10.1074/jbc.M210286200
Date:
30-Oct-02     Release date:   04-Feb-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P14668  (ANXA5_RAT) -  Annexin A5
Seq:
Struc:
319 a.a.
318 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     extracellular space   8 terms 
  Biological process     hemostasis   8 terms 
  Biochemical function     protein binding     5 terms  

 

 
DOI no: 10.1074/jbc.M210286200 J Biol Chem 278:2437-2443 (2003)
PubMed id: 12401794  
 
 
Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces.
Y.Mo, B.Campos, T.R.Mealy, L.Commodore, J.F.Head, J.R.Dedman, B.A.Seaton.
 
  ABSTRACT  
 
Annexin V is an abundant eukaryotic protein that binds phospholipid membranes in a Ca(2+)-dependent manner. In the present studies, site-directed mutagenesis was combined with x-ray crystallography and solution liposome binding assays to probe the functional role of a cluster of interfacial basic residues in annexin V. Four mutants were investigated: R23E, K27E, R61E, and R149E. All four mutants exhibited a significant reduction in adsorption to phospholipid membranes relative to the wild-type protein, and the R23E mutation was the most deleterious. Crystal structures of wild-type and mutant proteins were similar except for local changes in salt bridges involving basic cluster residues. The combined data indicate that Arg(23) is a major determinant for interfacial phospholipid binding and participates in an intermolecular salt bridge that is key for trimer formation on the membrane surface. Together, crystallographic and solution data provide evidence that the interfacial basic cluster is a locus where trimerization is synergistically coupled to membrane phospholipid binding.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Fluorescence (FRET ) assay comparing membrane binding by annexin V wild-type and mutants. Open circles, wild-type annexin V; squares, R149E; diamonds, K27E; triangles, R61E; closed circles, R23E.
Figure 5.
Fig. 5. Location of sulfate ion (space-filling representation) bound to the basic cluster in wild-type annexin V (ribbon representation), relative to membrane and subunit interfaces. a, annexin trimer (one molecule is shown in a darker shade with domains designated by Roman numerals), looking down the 3-fold axis, perpendicular to the plane of the membrane. b, subunit interface (trimer has been rotated 90° around the x-axis from the view in a). Small spheres, calcium ions.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 2437-2443) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21468022 A.Bouter, C.Gounou, R.Bérat, S.Tan, B.Gallois, T.Granier, B.L.d'Estaintot, E.Pöschl, B.Brachvogel, and A.R.Brisson (2011).
Annexin-A5 assembled into two-dimensional arrays promotes cell membrane repair.
  Nat Commun, 2, 270.  
19388055 J.Turnay, A.Guzmán-Aránguez, E.Lecona, J.I.Barrasa, N.Olmo, and M.A.Lizarbe (2009).
Key role of the N-terminus of chicken annexin A5 in vesicle aggregation.
  Protein Sci, 18, 1095-1106.  
19232551 M.Frank, S.Sodin-Semrl, S.Irman, B.Bozic, and B.Rozman (2009).
Beta2-glycoprotein I and annexin A5 phospholipid interactions: artificial and cell membranes.
  Autoimmun Rev, 9, 5.  
17485856 J.F.Chiou, M.D.Woon, S.N.Cheng, C.H.Hsu, S.C.Cherng, F.K.Hsieh, S.M.Lin, and C.Y.Shiau (2007).
Staphylokinase-annexin XI chimera exhibited efficient in vitro thrombolytic activities.
  Biosci Biotechnol Biochem, 71, 1122-1129.  
15170336 J.F.Andersen, N.P.Gudderra, I.M.Francischetti, J.G.Valenzuela, and J.M.Ribeiro (2004).
Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect.
  Biochemistry, 43, 6987-6994.  
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.