1dfa
From Proteopedia
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'''CRYSTAL STRUCTURE OF PI-SCEI IN C2 SPACE GROUP''' | '''CRYSTAL STRUCTURE OF PI-SCEI IN C2 SPACE GROUP''' | ||
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==Reference== | ==Reference== | ||
Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking., Hu D, Crist M, Duan X, Quiocho FA, Gimble FS, J Biol Chem. 2000 Jan 28;275(4):2705-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10644733 10644733] | Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking., Hu D, Crist M, Duan X, Quiocho FA, Gimble FS, J Biol Chem. 2000 Jan 28;275(4):2705-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10644733 10644733] | ||
| - | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Hu, D.]] | [[Category: Hu, D.]] | ||
[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
| - | [[Category: | + | [[Category: Homing endonuclease]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Intein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:47:15 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:47, 2 May 2008
CRYSTAL STRUCTURE OF PI-SCEI IN C2 SPACE GROUP
Overview
The PI-SceI protein is an intein-encoded homing endonuclease that initiates the mobility of its gene by making a double strand break at a single site in the yeast genome. The PI-SceI protein splicing and endonucleolytic active sites are separately located in each of two domains in the PI-SceI structure. To determine the spatial relationship between bases in the PI-SceI recognition sequence and selected PI-SceI amino acids, the PI-SceI-DNA complex was probed by photocross-linking and affinity cleavage methods. Unique solvent-accessible cysteine residues were introduced into the two PI-SceI domains at positions 91, 97, 170, 230, 376, and 378, and the mutant proteins were modified with either 4-azidophenacyl bromide or iron (S)-1-(p-bromoacetamidobenzyl)-ethylenediaminetetraacetate (FeBABE). The phenyl azide-coupled proteins cross-linked to the PI-SceI target sequence, and the FeBABE-modified proteins cleaved the DNA proximal to the derivatized amino acid. The results suggest that an extended beta-hairpin loop in the endonuclease domain that contains residues 376 and 378 contacts the major groove near the PI-SceI cleavage site. Conversely, residues 91, 97, and 170 in the protein splicing domain are in close proximity to a distant region of the substrate. To interpret our results, we used a new PI-SceI structure that is ordered in regions of the protein that bind DNA. The data strongly support a model of the PI-SceI-DNA complex derived from this structure.
About this Structure
1DFA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking., Hu D, Crist M, Duan X, Quiocho FA, Gimble FS, J Biol Chem. 2000 Jan 28;275(4):2705-12. PMID:10644733 Page seeded by OCA on Fri May 2 13:47:15 2008
