6imc: Difference between revisions

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'''Unreleased structure'''


The entry 6imc is ON HOLD  until Jan 22 2021
==Crystal Structure of ALKBH1 in complex with Mn(II) and N-Oxalylglycine==
 
<StructureSection load='6imc' size='340' side='right'caption='[[6imc]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
Authors: Zhang, M., Yang, S., Zhao, W., Li, H.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6imc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IMC FirstGlance]. <br>
Description: Crystal structure of Protein ZM
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ima|6ima]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6imc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6imc OCA], [http://pdbe.org/6imc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6imc RCSB], [http://www.ebi.ac.uk/pdbsum/6imc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6imc ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ALKB1_MOUSE ALKB1_MOUSE]] Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:27027282, PubMed:27745969). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:27027282). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (By similarity). Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (By similarity). In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at this position (By similarity). mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (By similarity). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:27027282). N(6)-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (PubMed:27027282). Demethylates mRNAs containing N(3)-methylcytidine modification (By similarity). Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity (By similarity). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (By similarity). DNA lyase activity does not require alpha-ketboglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (By similarity). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation (PubMed:23825659). May play a role in placental trophoblast lineage differentiation (PubMed:18163532).[UniProtKB:Q13686]<ref>PMID:18163532</ref> <ref>PMID:23825659</ref> <ref>PMID:27027282</ref> <ref>PMID:27745969</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Li, H]]
[[Category: Li, H]]
[[Category: Yang, S]]
[[Category: Zhang, M]]
[[Category: Zhang, M]]
[[Category: Zhao, W]]
[[Category: Zhao, W]]
[[Category: Yang, S]]
[[Category: Double-stranded beta helix]]
[[Category: Gene regulation]]

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