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1a74

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(New page: 200px<br /><applet load="1a74" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a74, resolution 2.200&Aring;" /> '''I-PPOL HOMING ENDON...)
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'''I-PPOL HOMING ENDONUCLEASE/DNA COMPLEX'''<br />
'''I-PPOL HOMING ENDONUCLEASE/DNA COMPLEX'''<br />
==Overview==
==Overview==
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Homing endonucleases are a diverse collection of proteins that are encoded, by genes with mobile, self-splicing introns. They have also been, identified in self-splicing inteins (protein introns). These enzymes, promote the movement of the DNA sequences that encode them from one, chromosome location to another; they do this by making a site-specific, double-strand break at a target site in an allele that lacks the, corresponding mobile intron. The target sites recognized by these small, endonucleases are generally long (14-44 base pairs). Four families of, homing endonucleases have been identified, including the LAGLIDADG, the, His-Cys box, the GIY-YIG and the H-N-H endonucleases. The first identified, His-Cys box homing endonuclease was I-PpoI from the slime mould Physarum, polycephalum. Its gene resides in one of only a few nuclear introns known, to exhibit genetic mobility. Here we report the structure of the I-PpoI, homing endonuclease bound to homing-site DNA determined to 1.8 A, resolution. I-PpoI displays an elongated fold of dimensions 25 x 35 x 80, A, with mixed alpha/beta topology. Each I-PpoI monomer contains three, antiparallel beta-sheets flanked by two long alpha-helices and a long, carboxy-terminal tail, and is stabilized by two bound zinc ions 15 A, apart. The enzyme possesses a new zinc-bound fold and endonuclease active, site. The structure has been determined in both uncleaved substrate and, cleaved product complexes.
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Homing endonucleases are a diverse collection of proteins that are encoded by genes with mobile, self-splicing introns. They have also been identified in self-splicing inteins (protein introns). These enzymes promote the movement of the DNA sequences that encode them from one chromosome location to another; they do this by making a site-specific double-strand break at a target site in an allele that lacks the corresponding mobile intron. The target sites recognized by these small endonucleases are generally long (14-44 base pairs). Four families of homing endonucleases have been identified, including the LAGLIDADG, the His-Cys box, the GIY-YIG and the H-N-H endonucleases. The first identified His-Cys box homing endonuclease was I-PpoI from the slime mould Physarum polycephalum. Its gene resides in one of only a few nuclear introns known to exhibit genetic mobility. Here we report the structure of the I-PpoI homing endonuclease bound to homing-site DNA determined to 1.8 A resolution. I-PpoI displays an elongated fold of dimensions 25 x 35 x 80 A, with mixed alpha/beta topology. Each I-PpoI monomer contains three antiparallel beta-sheets flanked by two long alpha-helices and a long carboxy-terminal tail, and is stabilized by two bound zinc ions 15 A apart. The enzyme possesses a new zinc-bound fold and endonuclease active site. The structure has been determined in both uncleaved substrate and cleaved product complexes.
==About this Structure==
==About this Structure==
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1A74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A74 OCA].
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1A74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A74 OCA].
==Reference==
==Reference==
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[[Category: Physarum polycephalum]]
[[Category: Physarum polycephalum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Flick, K.E.]]
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[[Category: Flick, K E.]]
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[[Category: Junior, R.J.Monnat.]]
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[[Category: Junior, R J.Monnat.]]
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[[Category: Jurica, B.L.]]
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[[Category: Jurica, B L.]]
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[[Category: Stoddard, M.S.]]
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[[Category: Stoddard, M S.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: complex (homing endonuclease/dna)]]
[[Category: complex (homing endonuclease/dna)]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:39:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:38 2008''

Revision as of 09:41, 21 February 2008


1a74, resolution 2.200Å

Drag the structure with the mouse to rotate

I-PPOL HOMING ENDONUCLEASE/DNA COMPLEX

Overview

Homing endonucleases are a diverse collection of proteins that are encoded by genes with mobile, self-splicing introns. They have also been identified in self-splicing inteins (protein introns). These enzymes promote the movement of the DNA sequences that encode them from one chromosome location to another; they do this by making a site-specific double-strand break at a target site in an allele that lacks the corresponding mobile intron. The target sites recognized by these small endonucleases are generally long (14-44 base pairs). Four families of homing endonucleases have been identified, including the LAGLIDADG, the His-Cys box, the GIY-YIG and the H-N-H endonucleases. The first identified His-Cys box homing endonuclease was I-PpoI from the slime mould Physarum polycephalum. Its gene resides in one of only a few nuclear introns known to exhibit genetic mobility. Here we report the structure of the I-PpoI homing endonuclease bound to homing-site DNA determined to 1.8 A resolution. I-PpoI displays an elongated fold of dimensions 25 x 35 x 80 A, with mixed alpha/beta topology. Each I-PpoI monomer contains three antiparallel beta-sheets flanked by two long alpha-helices and a long carboxy-terminal tail, and is stabilized by two bound zinc ions 15 A apart. The enzyme possesses a new zinc-bound fold and endonuclease active site. The structure has been determined in both uncleaved substrate and cleaved product complexes.

About this Structure

1A74 is a Single protein structure of sequence from Physarum polycephalum with as ligand. Full crystallographic information is available from OCA.

Reference

DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI., Flick KE, Jurica MS, Monnat RJ Jr, Stoddard BL, Nature. 1998 Jul 2;394(6688):96-101. PMID:9665136

Page seeded by OCA on Thu Feb 21 11:41:38 2008

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