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| {{STRUCTURE_1ef0| PDB=1ef0 | SCENE= }} | | {{STRUCTURE_1ef0| PDB=1ef0 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR'''
| | ===CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR=== |
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| ==Overview==
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| PI-SceI is a member of a class of proteins (inteins) that excise themselves from a precursor protein and in the process ligate the flanking protein sequences (exteins). We report here the 2.1-A resolution crystal structure of a PI-SceI miniprecursor (VMA29) containing 10 N-terminal extein residues and 4 C-terminal extein residues. Mutations at the N- and C-terminal splicing junctions, blocking in vivo protein splicing, allowed the miniprecursor to be purified and crystallized. The structure reveals both the N- and C-terminal scissile peptide bonds to be in distorted trans conformations (tau approximately 100 degrees ). Modeling of the wild-type PI-SceI based on the VMA29 structure indicates a large conformational change (movement of >9 A) must occur to allow transesterification to be completed. A zinc atom was discovered at the C-terminal splicing junction. Residues Cys(455), His(453), and Glu(80) along with a water molecule (Wat(53)) chelate the zinc atom. The crystal structure of VMA29 has captured the intein in its pre-spliced state.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10828056}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10828056 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10828056}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mini-precursor]] | | [[Category: Mini-precursor]] |
| [[Category: Protein splicing]] | | [[Category: Protein splicing]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:01:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:35:54 2008'' |