1vyb
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1vyb |SIZE=350|CAPTION= <scene name='initialview01'>1vyb</scene>, resolution 1.80Å | |PDB= 1vyb |SIZE=350|CAPTION= <scene name='initialview01'>1vyb</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyb OCA], [http://www.ebi.ac.uk/pdbsum/1vyb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vyb RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Repanas, K.]] | [[Category: Repanas, K.]] | ||
[[Category: Weichenrieder, O.]] | [[Category: Weichenrieder, O.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO3]] | ||
| - | [[Category: SO4]] | ||
[[Category: ape-1 type]] | [[Category: ape-1 type]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
| Line 35: | Line 35: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:28:40 2008'' |
Revision as of 21:28, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENDONUCLEASE DOMAIN OF HUMAN LINE1 ORF2P
Overview
The human L1 endonuclease (L1-EN) is encoded by the non-LTR retrotransposon LINE-1 (L1). L1 is responsible for more than 1.5 million retrotransposition events in the history of the human genome, contributing more than a quarter to human genomic DNA (L1 and Alu elements). L1-EN is related to the well-understood human DNA repair endonuclease APE1, and its nicking specificity is a major determinant for retrotransposon integration site selection. The crystal structure of human L1 endonuclease is the first of a retrotransposon-encoded protein and a prototype for retrotransposon-encoded endonucleases involved in target-primed reverse transcription. Structure-based endonuclease alignments reveal a conserved threonine in addition to previously identified invariant residues and suggest that DNA recognition proceeds via the accommodation of an extrahelical nucleotide within a pocket of the enzyme. The present analysis will help to refine phylogenetic and functional relationships among metal-dependent phosphohydrolases and provides a basis for manipulating non-LTR retrotransposon integration site selection.
About this Structure
1VYB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the targeting endonuclease of the human LINE-1 retrotransposon., Weichenrieder O, Repanas K, Perrakis A, Structure. 2004 Jun;12(6):975-86. PMID:15274918
Page seeded by OCA on Mon Mar 31 00:28:40 2008
