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PDBsum entry 1z1y

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protein metals Protein-protein interface(s) links
Cell adhesion PDB id
1z1y

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
177 a.a. *
Metals
_YB ×9
Waters ×88
* Residue conservation analysis
PDB id:
1z1y
Name: Cell adhesion
Title: Crystal structure of methylated pvs25, an ookinete protein from plasmodium vivax
Structure: Ookinete surface protein pvs25. Chain: a, b. Engineered: yes
Source: Plasmodium vivax. Malaria parasite p. Vivax. Organism_taxid: 5855. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Resolution:
2.00Å     R-factor:   0.245     R-free:   0.276
Authors: A.K.Saxena,K.Singh,H.P.Su,M.M.Klein,A.W.Stowers,A.J.Saul,C.A.Long, D.N.Garboczi
Key ref:
A.K.Saxena et al. (2006). The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms. Nat Struct Mol Biol, 13, 90-91. PubMed id: 16327807 DOI: 10.1038/nsmb1024
Date:
07-Mar-05     Release date:   06-Dec-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O96555  (O96555_PLAVI) -  Ookinete surface protein from Plasmodium vivax
Seq:
Struc:
219 a.a.
177 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 22 residue positions (black crosses)

 

 
DOI no: 10.1038/nsmb1024 Nat Struct Mol Biol 13:90-91 (2006)
PubMed id: 16327807  
 
 
The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms.
A.K.Saxena, K.Singh, H.P.Su, M.M.Klein, A.W.Stowers, A.J.Saul, C.A.Long, D.N.Garboczi.
 
  ABSTRACT  
 
P25 and P28 proteins are essential for Plasmodium parasites to infect mosquitoes and are leading candidates for a transmission-blocking malaria vaccine. The Plasmodium vivax P25 is a triangular prism that could tile the parasite surface. The residues forming the triangle are conserved in P25 and P28 from all Plasmodium species. A cocrystal structure shows that a transmission-blocking antibody uses only its heavy chain to bind Pvs25 at a vertex of the triangle.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Views of Pvs25. (a) The triangular prism formed by domain 1 (light blue), domain 2 (green), domain 3 (red) and domain 4 (gold). The central -strands in each domain are labeled 1 and 2. The 11 disulfide bonds (violet) are shown. (b) View of the edge of the prism. (c) Pvs25 forms sheets in the crystals. One molecule (red) makes contacts with four 2[1] symmetry mates (light blue) and two molecules related by lattice translations (dark blue). The six light blue molecules all have the same triangular face 'up', whereas the other three molecules (red and dark blue) all have the opposite face 'up'. As P25 and P28 molecules are thin prisms, the glycosylphosphatidylinositol anchor could reach the cell membrane whether a molecule was facing 'up' or 'down' on the membrane. N term, N terminus; C term, C terminus.
Figure 2.
Figure 2. Binding of transmission-blocking antibodies to Pvs25. (a) 2A8 Fab bound via its heavy chain (dark blue) to the B loop of Pvs25 domain 2. The light chain (light blue) does not contact Pvs25. The B loop of Pvs25 domain 3 (red) extends up from the plane of the triangle. (b) Monoclonal antibodies 1H10 and 1A5 do not bind in the presence of prebound 2A8. With Pvs25 immobilized on a Biacore chip, 2A8 was injected at (i) until binding was saturated at (ii), and then the second antibody and 2A8 were injected at (iii) until (iv). Buffer without protein was injected from (ii) to (iii) and from (iv) onward.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2006, 13, 90-91) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20584978 T.Miyata, T.Harakuni, T.Tsuboi, J.Sattabongkot, H.Kohama, M.Tachibana, G.Matsuzaki, M.Torii, and T.Arakawa (2010).
Plasmodium vivax ookinete surface protein Pvs25 linked to cholera toxin B subunit induces potent transmission-blocking immunity by intranasal as well as subcutaneous immunization.
  Infect Immun, 78, 3773-3782.  
19066995 B.Sharma, and M.K.Jaiswal (2009).
EGF domain II of protein Pb28 from Plasmodium berghei interacts with monoclonal transmission blocking antibody 13.1.
  J Mol Model, 15, 369-382.  
19057932 B.Sharma, and R.D.Ambedkar (2009).
A very large C-loop in EGF domain IV is characteristic of the P28 family of ookinete surface proteins.
  J Mol Model, 15, 309-321.  
19695097 R.M.Couñago, M.Davlieva, U.Strych, R.E.Hill, and K.L.Krause (2009).
Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames).
  BMC Struct Biol, 9, 53.
PDB code: 3ha1
18333885 P.R.Gilson, R.A.O'Donnell, T.Nebl, P.R.Sanders, M.E.Wickham, T.F.McElwain, T.F.de Koning-Ward, and B.S.Crabb (2008).
MSP1(19) miniproteins can serve as targets for invasion inhibitory antibodies in Plasmodium falciparum provided they contain the correct domains for cell surface trafficking.
  Mol Microbiol, 68, 124-138.  
18248630 P.Srinivasan, H.Fujioka, and M.Jacobs-Lorena (2008).
PbCap380, a novel oocyst capsule protein, is essential for malaria parasite survival in the mosquito.
  Cell Microbiol, 10, 1304-1312.  
17557884 A.K.Saxena, Y.Wu, and D.N.Garboczi (2007).
Plasmodium p25 and p28 surface proteins: potential transmission-blocking vaccines.
  Eukaryot Cell, 6, 1260-1265.  
17762780 A.Saul (2007).
Mosquito stage, transmission blocking vaccines for malaria.
  Curr Opin Infect Dis, 20, 476-481.  
17686163 K.Miura, D.B.Keister, O.V.Muratova, J.Sattabongkot, C.A.Long, and A.Saul (2007).
Transmission-blocking activity induced by malaria vaccine candidates Pfs25/Pvs25 is a direct and predictable function of antibody titer.
  Malar J, 6, 107.  
17875391 P.Gayathri, H.Balaram, and M.R.Murthy (2007).
Structural biology of plasmodial proteins.
  Curr Opin Struct Biol, 17, 744-754.  
18074396 R.L.Rich, and D.G.Myszka (2007).
Survey of the year 2006 commercial optical biosensor literature.
  J Mol Recognit, 20, 300-366.  
16797221 G.A.Bentley (2006).
Functional and immunological insights from the three-dimensional structures of Plasmodium surface proteins.
  Curr Opin Microbiol, 9, 395-400.  
16603068 J.Huang, and W.Honda (2006).
CED: a conformational epitope database.
  BMC Immunol, 7, 7.  
17098187 T.S.Walter, C.Meier, R.Assenberg, K.F.Au, J.Ren, A.Verma, J.E.Nettleship, R.J.Owens, D.I.Stuart, and J.M.Grimes (2006).
Lysine methylation as a routine rescue strategy for protein crystallization.
  Structure, 14, 1617-1622.  
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 code is shown on the right.

 

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