1at0
From Proteopedia
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==Overview== | ==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, . | + | 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== | ==About this Structure== | ||
| - | 1AT0 is a | + | 1AT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AT0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: developmental signaling molecule]] | [[Category: developmental signaling molecule]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:22:39 2007'' |
Revision as of 12:17, 5 November 2007
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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. Structure known Active Site: ACT. 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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