1AT0

17-kDA fragment of hedgehog C-terminal autoprocessing domain

Summary for 1AT0

• Entry DOI: 10.2210/pdb1at0/pdb
• Descriptor: 17-HEDGEHOG (2 entities in total)
• Functional Keywords: developmental signaling molecule, cholesterol transfer, signaling protein
• Biological source: Drosophila melanogaster (FRUIT FLY)
• Cellular location: Nucleus . Protein hedgehog N-product: Cell membrane ; Lipid-anchor . Protein hedgehog C-product: Secreted, extracellular space : Q02936
• Total number of polymer chains: 1
• Total formula weight: 15985.78

Authors

Hall, T.M.T.,Porter, J.A.,Young, K.E.,Koonin, E.V.,Beachy, P.A.,Leahy, D.J. (deposition date: 1997-08-15, release date: 1997-11-12, Last modification date: 2024-10-16)

Primary citation

Hall, T.M.,Porter, J.A.,Young, K.E.,Koonin, E.V.,Beachy, P.A.,Leahy, D.J.
Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins.
Cell(Cambridge,Mass.), 91:85-97, 1997

PubMed Abstract: 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.

PubMed: 9335337
DOI: 10.1016/S0092-8674(01)80011-8

Experimental method

X-RAY DIFFRACTION (1.9 Å)