1at0
From Proteopedia
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN
Overview
The approximately 25 kDa carboxy-terminal domain of Drosophila Hedgehog protein (Hh-C) possesses an autoprocessing activity that results in an intramolecular cleavage of full-length Hedgehog protein and covalent attachment of a cholesterol moiety to the newly generated amino-terminal fragment. We have identified a 17 kDa fragment of Hh-C (Hh-C17) active in the initiation of autoprocessing and report here its crystal structure. The Hh-C17 structure comprises two homologous subdomains that appear to have arisen from tandem duplication of a primordial gene. Residues in the Hh-C17 active site have been identified, and their role in Hedgehog autoprocessing probed by site-directed mutagenesis. Aspects of sequence, structure, and reaction mechanism are conserved between Hh-C17 and the self-splicing regions of inteins, permitting reconstruction of a plausible evolutionary history of Hh-C and the inteins.
About this Structure
1AT0 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins., Hall TM, Porter JA, Young KE, Koonin EV, Beachy PA, Leahy DJ, Cell. 1997 Oct 3;91(1):85-97. PMID:9335337
Page seeded by OCA on Sun Mar 30 18:46:59 2008
