1at0
From Proteopedia
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| - | [[Image:1at0.gif|left|200px]] | + | [[Image:1at0.gif|left|200px]] |
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| - | '''17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN''' | + | {{Structure |
| + | |PDB= 1at0 |SIZE=350|CAPTION= <scene name='initialview01'>1at0</scene>, resolution 1.9Å | ||
| + | |SITE= <scene name='pdbsite=ACT:Autoprocessing+Active+Site'>ACT</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''17-KDA FRAGMENT OF HEDGEHOG C-TERMINAL AUTOPROCESSING DOMAIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AT0 is a [ | + | 1AT0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AT0 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9335337 9335337] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: developmental signaling molecule]] | [[Category: developmental signaling molecule]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:59 2008'' |
Revision as of 08:02, 20 March 2008
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| 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
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