7jl5: Difference between revisions

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'''Unreleased structure'''


The entry 7jl5 is ON HOLD  until Paper Publication
==Crystal structure of human NEIL3 tandem zinc finger GRF domains==
 
<StructureSection load='7jl5' size='340' side='right'caption='[[7jl5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
Authors: Rodriguez, A.A., Wojtaszek, J.L., Williams, R.S., Eichman, B.F.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[7jl5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JL5 FirstGlance]. <br>
Description: Crystal structure of human NEIL3 tandem zinc finger GRF domains
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Rodriguez, A.A]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7jl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jl5 OCA], [https://pdbe.org/7jl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jl5 RCSB], [https://www.ebi.ac.uk/pdbsum/7jl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jl5 ProSAT]</span></td></tr>
[[Category: Wojtaszek, J.L]]
</table>
[[Category: Eichman, B.F]]
== Function ==
[[Category: Williams, R.S]]
[https://www.uniprot.org/uniprot/NEIL3_HUMAN NEIL3_HUMAN] DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair.<ref>PMID:12433996</ref> <ref>PMID:19170771</ref> <ref>PMID:22569481</ref> <ref>PMID:23755964</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Eichman BF]]
[[Category: Rodriguez AA]]
[[Category: Williams RS]]
[[Category: Wojtaszek JL]]

Latest revision as of 17:52, 6 March 2024

Crystal structure of human NEIL3 tandem zinc finger GRF domainsCrystal structure of human NEIL3 tandem zinc finger GRF domains

Structural highlights

7jl5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NEIL3_HUMAN DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair.[1] [2] [3] [4]

References

  1. ↑ Morland I, Rolseth V, Luna L, Rognes T, Bjoras M, Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res. 2002 Nov 15;30(22):4926-36. PMID:12433996
  2. ↑ Takao M, Oohata Y, Kitadokoro K, Kobayashi K, Iwai S, Yasui A, Yonei S, Zhang QM. Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant. Genes Cells. 2009 Feb;14(2):261-70. Epub 2008 Jan 15. PMID:19170771 doi:10.1111/j.1365-2443.2008.01271.x
  3. ↑ Liu M, Bandaru V, Holmes A, Averill AM, Cannan W, Wallace SS. Expression and purification of active mouse and human NEIL3 proteins. Protein Expr Purif. 2012 Jul;84(1):130-9. doi: 10.1016/j.pep.2012.04.022. Epub, 2012 May 5. PMID:22569481 doi:http://dx.doi.org/10.1016/j.pep.2012.04.022
  4. ↑ Krokeide SZ, Laerdahl JK, Salah M, Luna L, Cederkvist FH, Fleming AM, Burrows CJ, Dalhus B, Bjoras M. Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin. DNA Repair (Amst). 2013 Dec;12(12):1159-64. doi: 10.1016/j.dnarep.2013.04.026., Epub 2013 Jun 5. PMID:23755964 doi:http://dx.doi.org/10.1016/j.dnarep.2013.04.026

7jl5, resolution 2.60Å

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