Conserved Protein Domain Family
ACD_ScHsp26_like

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cd06472: ACD_ScHsp26_like 
Click on image for an interactive view with Cn3D
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.
Statistics
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PSSM-Id: 107229
View PSSM: cd06472
Aligned: 19 rows
Threshold Bit Score: 125.495
Threshold Setting Gi: 115464729
Created: 18-Mar-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interface
Conserved site includes 27 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:2H50, Saccharomyces cerevisiae Hsp26 dimer interface, contacts at 3.5 A
    View structure with Cn3D
  • Comment:ScHsp26 assembles in shell-like particles composed of 24 subunits. These particles are storage forms which upon heat shock disassociate into dimers. Non-native substrate proteins bind the disassociated ScHsp26 and assemble into large globular assemblies having one monomer of substrate bound per dimer.
  • Structure:1GME_A, Triticum aestivum sHsp dimer interface, contacts at 3.5 A
    View structure with Cn3D
  • Comment:T. aestivum HSP16.9 assembles as a 12-mer, comprised of two discs, each disc having 6 alpha crystallin-like domains organized as a trimer of dimers.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #######      # # ##                      #    #      #########      #    #      
2H50_A         2 RMDWKETPEAHVFKADLPGVKKEEVKVEVEDg-nVLVVSGERTKEKEDk----NDKWHRVERs-----SGKFVRRFRLLE 71
gi 123562     76 RVDWKETPEGHVIMVDVPGLKKDDIKIEVEEn-rVLRVSGERKKEEDKk----GDHWHRVERs-----YGKFWRQFKLPQ 145
gi 168036473  53 SVDWKETATEHVIKADVPGLSKNEIKVEVDDtqrVLRINGERRKEEERq----TDEWHVLERg-----DARYLRQLALPE 123
gi 116793157  27 QVDWLETPNAHIFKVNVPGMNKDDIKIQVEDg-hILHIKGEGKKEEDKt----EGMWHCMERg-----RGSFSRQFGLPE 96
gi 15240308   23 LIDWMESNNSHIFKINVPGYNKEDIKVQIEEg-nVLSIRGEGIKEEKKe----NLVWHVAEReafsggGSEFLRRIELPE 97
gi 116310226  77 RVDWRETGDAHEVVVDVPGMRKEDLRVEVEDn-rVLRISGERRREETTeqkggGDHWHREERs-----YGRFWRQLRLPD 150
gi 168063824   2 RMDWRETADAHILKTDMPGVRSDDVKVQVIDg-eVVEISGTRKKEEPKe----GDEWHHVERp-----SGFFFRSFRIPE 71
gi 148615645  45 KIYMKETAEAHVIKMEVPGLKREEVKVELEEg-nTVKICGEKIVEREEr----NGYWYRVERs-----GGRFVRSIRLPE 114
gi 116793760  79 HVDWWESSDAHIIQADLPGATKDDVEIIVENg-rVLQISGRSKMAVPPg----GGRCRRGERs-----RVGYLRRLRLPS 148
gi 115464729  94 TVDWAETDSEYYLRADIPGGRKCDVEVSGDDamrVVDVSGLWRAAPPPpp-pdGRDWRAGRWw-----EHGFVRRVELPE 167
                         90       100
                 ....*....|....*....|....
Feature 1                    #  ##       
2H50_A        72 DAKVEEVKAGLEN--GVLTVTVPK 93
gi 123562    146 NVDLDSVKAKMEN--GVLTLTLHK 167
gi 168036473 124 NANLDQITASVDN--GVLTVTMPK 145
gi 116793157  97 DVKMDHIKAQVEN--GVLTIIAPK 118
gi 15240308   98 NVKVDQVKAYVEN--GVLTVVVPK 119
gi 116310226 151 NADLDSIAASLDN--GVLTVRFRK 172
gi 168063824  72 NAKADDLKAQVAD--GVLTITLPK 93
gi 148615645 115 NANGQEMKACLDN--GVLFITVPK 136
gi 116793760 149 NADAEQLKAEMEN--GVLTVTIPK 170
gi 115464729 168 DADWRKVEAFFDDgeGLLEIKVPK 191

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