1lwt

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Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA (Ca2+ free)

Structural highlights

1lwt is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:MSE
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VATA_YEAST Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.[1] PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The first X-ray structures of an intein-DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca(2+). The DNA shows an asymmetric bending pattern, with a major 50 degree bend in the endonuclease domain and a minor 22 degree bend in the splicing domain region. Distortions of the DNA bound to the endonuclease domain cause the insertion of the two cleavage sites in the catalytic center. DNA binding induces changes in the protein conformation. The two overlapping non-identical active sites in the endonucleolytic center contain two Ca(+2) ions that coordinate to the catalytic Asp residues. Structure analysis indicates that the top strand may be cleaved first.

Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence.,Moure CM, Gimble FS, Quiocho FA Nat Struct Biol. 2002 Oct;9(10):764-70. PMID:12219083[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
12 reviews cite this structure
Meganucleases and other tools for targeted genome engineering: perspectives and challenges for gene therapy.
Silva et al. (2011)
11 more
49 other articles
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See Also

References

  1. ↑ Gimble FS, Thorner J. Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae. Nature. 1992 May 28;357(6376):301-6. PMID:1534148 doi:http://dx.doi.org/10.1038/357301a0
  2. ↑ Gimble FS, Thorner J. Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae. Nature. 1992 May 28;357(6376):301-6. PMID:1534148 doi:http://dx.doi.org/10.1038/357301a0
  3. ↑ Moure CM, Gimble FS, Quiocho FA. Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence. Nat Struct Biol. 2002 Oct;9(10):764-70. PMID:12219083 doi:10.1038/nsb840

Contents


PDB ID 1lwt

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