1at0
From Proteopedia
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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. Known structural/functional Site: . 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
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