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1at0
From Proteopedia
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| - | [[Image:1at0.gif|left|200px]]<br /> | + | [[Image:1at0.gif|left|200px]]<br /><applet load="1at0" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1at0" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1at0, resolution 1.9Å" /> | caption="1at0, resolution 1.9Å" /> | ||
'''17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN'''<br /> | '''17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. | + | 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]. Known structural/functional Site: <scene name='pdbsite=ACT:Autoprocessing Active Site'>ACT</scene>. 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 Tue Dec 18 14:21:05 2007'' |
Revision as of 12:11, 18 December 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. 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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