1at0
From Proteopedia
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'''17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN''' | '''17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN''' | ||
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[[Category: Porter, J A.]] | [[Category: Porter, J A.]] | ||
[[Category: Young, K E.]] | [[Category: Young, K E.]] | ||
| - | [[Category: | + | [[Category: Cholesterol transfer]] |
| - | [[Category: | + | [[Category: Developmental signaling molecule]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:39:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:39, 2 May 2008
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 Fri May 2 10:39:37 2008
