Summary: Beta/Gamma crystallin
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Members of this family assume a beta-gamma-crystallin fold [1,2], wherein nine beta-strands are connected by loop, and are separated into two sheets, each sheet forming the Greek key motif. The two Greek key motifs face each other in the global topology. The three-dimensional structure of the molecule is a 'sandwich'-shaped beta-barrel structure: hydrophobic side-chains are packed in the large interface area of the beta-sheets. In Streptomyces killer toxin-like protein domain confers a cytocidal effect to the toxin, causing cell death in both budding and fission yeasts, and morphological changes in yeasts and filamentous fungi . This family also includes chitin-biding antifungal proteins [2-3].
Ohki SY, Kariya E, Hiraga K, Wakamiya A, Isobe T, Oda K, Kainosho M; , J Mol Biol. 2001;305:109-120.: NMR structure of Streptomyces killer toxin-like protein, SKLP: further evidence for the wide distribution of single-domain betagamma-crystallin superfamily proteins. PUBMED:11114251 EPMC:11114251
Campos-Olivas R, Horr I, Bormann C, Jung G, Gronenborn AM;, J Mol Biol. 2001;308:765-782.: Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901. PUBMED:11350173 EPMC:11350173
Bormann C, Baier D, Horr I, Raps C, Berger J, Jung G, Schwarz H;, J Bacteriol. 1999;181:7421-7429.: Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity. PUBMED:10601197 EPMC:10601197
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015161
This domain consists of a beta-gamma-crystallin fold [PUBMED:11114251, PUBMED:11350173], wherein nine beta-strands are connected by loop, and are separated into two sheets, each sheet forming the Greek key motif. The two Greek key motifs face each other in the global topology. The three-dimensional structure of the molecule is a 'sandwich'-shaped beta-barrel structure: hydrophobic side-chains are packed in the large interface area of the beta-sheets. In Streptomyces killer toxin-like protein domain confers a cytocidal effect to the toxin, causing cell death in both budding and fission yeasts, and morphological changes in yeasts and filamentous fungi [PUBMED:11114251]. This domain is also found in chitin-biding antifungal proteins [PUBMED:11350173, PUBMED:10601197].
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This superfamily includes a number of mammalian crystallins as well as ancestral beta gamma-crystallin precursor structures.
The clan contains the following 6 members:Crystall Crystall_2 Crystall_3 Inhibitor_I36 MiAMP1 Yeast-kill-tox
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Sammut SJ, Eberhardt R|
|Number in seed:||7|
|Number in full:||12|
|Average length of the domain:||70.70 aa|
|Average identity of full alignment:||43 %|
|Average coverage of the sequence by the domain:||64.29 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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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 Crystall_2 domain has been found. There are 2 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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