1af5
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1af5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1af5 OCA], [http://www.ebi.ac.uk/pdbsum/1af5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1af5 RCSB]</span> | ||
}} | }} | ||
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[[Category: laglidadg motif]] | [[Category: laglidadg motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:38:56 2008'' |
Revision as of 15:38, 30 March 2008
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| , resolution 3.00Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GROUP I MOBILE INTRON ENDONUCLEASE
Overview
The structure of I-Crel provides the first view of a protein encoded by a gene within an intron. This endonuclease recognizes a long DNA site approximately 20 base pairs in length and facilitates the lateral transfer of that intron. The protein exhibits a DNA-binding surface consisting of four antiparallel beta-strands that form a 20 A wide groove which is over 70 A long. The architecture of this fold is different from that of the TATA binding protein, TBP, which also contains an antiparallel beta-saddle. The conserved LAGLIDADG motif, which is found in many mobile intron endonucleases, maturases and inteins, forms a novel helical interface and contributes essential residues to the active site.
About this Structure
1AF5 is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
The structure of I-Crel, a group I intron-encoded homing endonuclease., Heath PJ, Stephens KM, Monnat RJ Jr, Stoddard BL, Nat Struct Biol. 1997 Jun;4(6):468-76. PMID:9187655
Page seeded by OCA on Sun Mar 30 18:38:56 2008
