1ef0: Difference between revisions
New page: left|200px<br /><applet load="1ef0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ef0, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1ef0.jpg|left|200px]]<br /><applet load="1ef0" size=" | [[Image:1ef0.jpg|left|200px]]<br /><applet load="1ef0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ef0, resolution 2.1Å" /> | caption="1ef0, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR'''<br /> | '''CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR'''<br /> | ||
==Overview== | ==Overview== | ||
PI-SceI is a member of a class of proteins (inteins) that excise | 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. | ||
==About this Structure== | ==About this Structure== | ||
1EF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http:// | 1EF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EF0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Poland, B | [[Category: Poland, B W.]] | ||
[[Category: Quiocho, F | [[Category: Quiocho, F A.]] | ||
[[Category: Xu, M | [[Category: Xu, M Q.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
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[[Category: protein splicing]] | [[Category: protein splicing]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:04 2008'' | ||
Revision as of 10:27, 21 February 2008
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CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR
Overview
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.
About this Structure
1EF0 is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Structural insights into the protein splicing mechanism of PI-SceI., Poland BW, Xu MQ, Quiocho FA, J Biol Chem. 2000 Jun 2;275(22):16408-13. PMID:10828056
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