1gpp: Difference between revisions

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|SITE=  
|SITE=  
|LIGAND=  
|LIGAND=  
|ACTIVITY= [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]  
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpp OCA], [http://www.ebi.ac.uk/pdbsum/1gpp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gpp RCSB]</span>
}}
}}


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[[Category: protein splicing]]
[[Category: protein splicing]]


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Revision as of 20:49, 30 March 2008

File:1gpp.gif


PDB ID 1gpp

Drag the structure with the mouse to rotate
, resolution 1.35Å
Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE S.CEREVISIAE HOMING ENDONUCLEASE PI-SCEI DOMAIN I


OverviewOverview

The homing endonuclease PI-SceI from Saccharo myces cerevisiae consists of two domains. The protein splicing domain I catalyzes the excision of the mature endonuclease (intein) from a precursor protein and the religation of the flanking amino acid sequences (exteins) to a functional protein. Furthermore, domain I is involved in binding and recognition of the specific DNA substrate. Domain II of PI-SceI, the endonuclease domain, which is structurally homologous to other homing endonucleases from the LAGLIDADG family, harbors the endonucleolytic center of PI-SceI, which in vivo initiates the homing process by introducing a double-strand cut in the approximately 35 bp recognition sequence. At 1.35 A resolution, the crystal structure of PI-SceI domain I provides a detailed view of the part of the protein that is responsible for tight and specific DNA binding. A geometry-based docking of the 75 degrees bent recognition sequence to the full-length protein implies a conformational change or hinge movement of a subdomain of domain I, the tongs part, that is predicted to reach into the major groove near base pairs +16 to +18.

About this StructureAbout this Structure

1GPP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI., Werner E, Wende W, Pingoud A, Heinemann U, Nucleic Acids Res. 2002 Sep 15;30(18):3962-71. PMID:12235380

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