3gw6

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3gw6, resolution 2.60Å ()
Ligands: , , , ,
Gene: sia, 17, 17.0 (Enterobacteria phage K1F)
Activity: Endo-alpha-sialidase, with EC number 3.2.1.129
Related: 3gud
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Intramolecular Chaperone

Publication Abstract from PubMed

Protein folding is often mediated by molecular chaperones. Recently, a novel class of intramolecular chaperones has been identified in tailspike proteins of evolutionarily distant viruses, which require a C-terminal chaperone for correct folding. The highly homologous chaperone domains are interchangeable between pre-proteins and release themselves after protein folding. Here we report the crystal structures of two intramolecular chaperone domains in either the released or the pre-cleaved form, revealing the role of the chaperone domain in the formation of a triple-beta-helix fold. Tentacle-like protrusions enclose the polypeptide chains of the pre-protein during the folding process. After the assembly, a sensory mechanism for correctly folded beta-helices triggers a serine-lysine catalytic dyad to autoproteolytically release the mature protein. Sequence analysis shows a conservation of the intramolecular chaperones in functionally unrelated proteins sharing beta-helices as a common structural motif.

Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding., Schulz EC, Dickmanns A, Urlaub H, Schmitt A, Muhlenhoff M, Stummeyer K, Schwarzer D, Gerardy-Schahn R, Ficner R, Nat Struct Mol Biol. 2010 Feb;17(2):210-5. Epub 2010 Jan 31. PMID:20118935

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3gw6 is a 6 chain structure with sequence from Enterobacteria phage k1f. Full crystallographic information is available from OCA.

See Also

Reference

  • Schulz EC, Dickmanns A, Urlaub H, Schmitt A, Muhlenhoff M, Stummeyer K, Schwarzer D, Gerardy-Schahn R, Ficner R. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nat Struct Mol Biol. 2010 Feb;17(2):210-5. Epub 2010 Jan 31. PMID:20118935 doi:10.1038/nsmb.1746

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