2op6

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Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegansPeptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans

Structural highlights

2op6 is a 1 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

BIBH_CAEEL Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions (PubMed:15716356). Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion (PubMed:15716356).[UniProtKB:P11021][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Poteryaev D, Squirrell JM, Campbell JM, White JG, Spang A. Involvement of the actin cytoskeleton and homotypic membrane fusion in ER dynamics in Caenorhabditis elegans. Mol Biol Cell. 2005 May;16(5):2139-53. PMID:15716356 doi:10.1091/mbc.e04-08-0726

2op6, resolution 1.85Å

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OCA