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11  structures 40  species 0  interactions 77  sequences 1  architecture

Family: Egg_lysin (PF01303)

Summary: Egg lysin (Sperm-lysin)

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Egg lysin Edit Wikipedia article

Egg lysin (Sperm-lysin)
Identifiers
Symbol Egg_lysin
Pfam PF01303
InterPro IPR001379
SCOP 1lis
SUPERFAMILY 1lis

Egg lysin is a protein that creates a hole in the envelope of the egg thereby allowing the sperm to pass through the envelope and fuse with the egg.

Fertilization proteins are acrosomal proteins involved in various roles during the fertilization process. Structurally these proteins consist of a closed bundle of helices with a right-hand twist. Lysin and SP18, both characterised in abalone, are two evolutionarily related fertilization proteins that have distinctive roles.

Following its release from sperm, lysin binds to the egg vitelline envelope (VE) via the VE receptor for lysin (VERL), then non-enzymatically dissolves the VE to create a hole, thereby allowing the sperm to pass through the envelope and fuse with the egg.[1] Lysins exhibit species-specific binding to their egg receptor, possibly through differences in charged surface residues.[2] SP18 is also released from sperm, acting as a potent fusagen of liposomes to mediate the fusion between the sperm and egg cell membranes. Despite a similarity in the overall fold, the variation in the surface features of SP18 and lysin account for their different roles in fertilization.[3]

[edit] References

  1. ^ Stout CD, Vacquier VD, Kresge N (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 56: 34–41. PMID 10666624. 
  2. ^ Stout CD, Vacquier VD, Kresge N (2000). "The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor". J. Mol. Biol. 296 (5): 1225–1234. doi:10.1006/jmbi.2000.3533. PMID 10698629. 
  3. ^ Stout CD, Vacquier VD, Kresge N (2001). "The crystal structure of a fusagenic sperm protein reveals extreme surface properties". Biochemistry 40 (18): 5407–5413. doi:10.1021/bi002779v. PMID 11331004. 

This article incorporates text from the public domain Pfam and InterPro IPR001379

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Egg lysin (Sperm-lysin) Provide feedback

Egg lysin creates a hole in the envelope of the egg thereby allowing the sperm to pass through the envelope and fuse with the egg.

Literature references

  1. Shaw A, McRee DE, Vacquier VD, Stout CD; , Science 1993;262:1864-1867.: The crystal structure of lysin, a fertilization protein. PUBMED:8266073 EPMC:8266073

  2. Shaw A, Fortes PA, Stout CD, Vacquier VD; , J Cell Biol 1995;130:1117-1125.: Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species. PUBMED:7657696 EPMC:7657696


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001379

Fertilization proteins are acrosomal proteins involved in various roles during the fertilization process. Structurally these proteins consist of a closed bundle of helices with a right-hand twist. Lysin and SP18, both characterised in abalone, are two evolutionarily related fertilization proteins that have distinctive roles. Following its release from sperm, lysin binds to the egg vitelline envelope (VE) via the VE receptor for lysin (VERL), then non-enzymatically dissolves the VE to create a hole, thereby allowing the sperm to pass through the envelope and fuse with the egg [PUBMED:10666624]. Lysins exhibit species-specific binding to their egg receptor, possibly through differences in charged surface residues [PUBMED:10698629]. SP18 is also released from sperm, acting as a potent fusagen of liposomes to mediate the fusion between the sperm and egg cell membranes. Despite a similarity in the overall fold, the variation in the surface features of SP18 and lysin account for their different roles in fertilization [PUBMED:11331004].

Gene Ontology

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Domain organisation

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Alignments

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RP55
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(24)
Full
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Representative proteomes NCBI
(85)
Meta
(0)
RP15
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RP35
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RP55
(2)
RP75
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Seed source: Pfam-B_1464 (release 3.0)
Previous IDs: none
Type: Domain
Author: Finn RD, Bateman A
Number in seed: 24
Number in full: 77
Average length of the domain: 88.00 aa
Average identity of full alignment: 52 %
Average coverage of the sequence by the domain: 83.19 %

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HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.1 21.1
Noise cut-off 20.6 20.6
Model length: 121
Family (HMM) version: 12
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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Egg_lysin domain has been found. There are 11 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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