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PDBsum entry 1lis

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protein links
Fertilization protein PDB id
1lis
Jmol
Contents
Protein chain
131 a.a. *
Waters ×84
* Residue conservation analysis
PDB id:
1lis
Name: Fertilization protein
Title: The crystal structure of a fertilization protein
Structure: Lysin. Chain: a. Engineered: yes
Source: Haliotis rufescens. California red abalone. Organism_taxid: 6454
Resolution:
1.90Å     R-factor:   0.187    
Authors: A.Shaw,D.E.Mcree,V.D.Vacquier,C.D.Stout
Key ref: A.Shaw et al. (1993). The crystal structure of lysin, a fertilization protein. Science, 262, 1864-1867. PubMed id: 8266073 DOI: 10.1126/science.8266073
Date:
29-Jun-93     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04552  (ELYS_HALRU) -  Egg-lysin
Seq:
Struc:
154 a.a.
131 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     single fertilization   1 term 

 

 
DOI no: 10.1126/science.8266073 Science 262:1864-1867 (1993)
PubMed id: 8266073  
 
 
The crystal structure of lysin, a fertilization protein.
A.Shaw, D.E.McRee, V.D.Vacquier, C.D.Stout.
 
  ABSTRACT  
 
Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg. The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20847216 S.Datta, R.Prado, A.Rodríguez, and A.A.Escalante (2010).
Characterizing molecular adaptation: a hierarchical approach to assess the selective influence of amino acid properties.
  Bioinformatics, 26, 2818-2825.  
17033626 M.A.Noor, and J.L.Feder (2006).
Speciation genetics: evolving approaches.
  Nat Rev Genet, 7, 851-861.  
16542458 W.S.Wong, R.Sainudiin, and R.Nielsen (2006).
Identification of physicochemical selective pressure on protein encoding nucleotide sequences.
  BMC Bioinformatics, 7, 148.  
11135314 N.Kresge, V.D.Vacquier, and C.D.Stout (2001).
Abalone lysin: the dissolving and evolving sperm protein.
  Bioessays, 23, 95.  
10666624 N.Kresge, V.D.Vacquier, and C.D.Stout (2000).
1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding.
  Acta Crystallogr D Biol Crystallogr, 56, 34-41.
PDB codes: 2lis 2lyn
10570982 H.Akashi (1999).
Within- and between-species DNA sequence variation and the 'footprint' of natural selection.
  Gene, 238, 39-51.  
10535974 S.R.Palumbi (1999).
All males are not created equal: fertility differences depend on gamete recognition polymorphisms in sea urchins.
  Proc Natl Acad Sci U S A, 96, 12632-12637.  
9565750 J.P.Schneider, A.Lombardi, and W.F.DeGrado (1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
  Fold Des, 3, R29-R40.  
  9655345 J.W.Bryson, J.R.Desjarlais, T.M.Handel, and W.F.DeGrado (1998).
From coiled coils to small globular proteins: design of a native-like three-helix bundle.
  Protein Sci, 7, 1404-1414.  
9182993 D.Willbold, S.Hoffmann, and P.Rösch (1997).
Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.
  Eur J Biochem, 245, 581-588.
PDB code: 1vpu
9261069 P.Sliz, R.Engelmann, W.Hengstenberg, and E.F.Pai (1997).
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
  Structure, 5, 775-788.
PDB code: 1e2a
9071007 V.D.Vacquier, W.J.Swanson, and Y.H.Lee (1997).
Positive Darwinian selection on two homologous fertilization proteins: what is the selective pressure driving their divergence?
  J Mol Evol, 44, S15-S22.  
9192632 W.J.Swanson, and V.D.Vacquier (1997).
The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule.
  Proc Natl Acad Sci U S A, 94, 6724-6729.  
8874031 S.Kumar, and M.Bansal (1996).
Structural and sequence characteristics of long alpha helices in globular proteins.
  Biophys J, 71, 1574-1586.  
7657696 A.Shaw, P.A.Fortes, C.D.Stout, and V.D.Vacquier (1995).
Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species.
  J Cell Biol, 130, 1117-1125.
PDB code: 1lyn
7576617 N.M.Mozingo, V.D.Vacquier, and D.E.Chandler (1995).
Structural features of the abalone egg extracellular matrix and its role in gamete interaction during fertilization.
  Mol Reprod Dev, 41, 493-502.  
8634069 R.J.Belton, and K.R.Foltz (1995).
Gamete and immune cell recognition revisited.
  Bioessays, 17, 1075-1080.  
7761431 W.J.Swanson, and V.D.Vacquier (1995).
Extraordinary divergence and positive Darwinian selection in a fusagenic protein coating the acrosomal process of abalone spermatozoa.
  Proc Natl Acad Sci U S A, 92, 4957-4961.  
7850426 W.Messier, and C.B.Stewart (1994).
Molecular evolution. Dissolving the barriers.
  Curr Biol, 4, 911-913.  
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.