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| | <StructureSection load='6d7n' size='340' side='right'caption='[[6d7n]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='6d7n' size='340' side='right'caption='[[6d7n]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d7n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Blackwell_switchgrass Blackwell switchgrass]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D7N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d7n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Panicum_virgatum Panicum virgatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D7N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=38727 Blackwell switchgrass])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d7n OCA], [https://pdbe.org/6d7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d7n RCSB], [https://www.ebi.ac.uk/pdbsum/6d7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d7n ProSAT]</span></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=6d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d7n OCA], [http://pdbe.org/6d7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d7n RCSB], [http://www.ebi.ac.uk/pdbsum/6d7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d7n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A1S4NYF8_PANVG A0A1S4NYF8_PANVG]] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.[RuleBase:RU362060] | + | [https://www.uniprot.org/uniprot/IMA1_MOUSE IMA1_MOUSE] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Blackwell switchgrass]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxidase]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gabel, S A]] | + | [[Category: Panicum virgatum]] |
| - | [[Category: London, R E]] | + | [[Category: Gabel SA]] |
| - | [[Category: Pedersen, L C]] | + | [[Category: London RE]] |
| - | [[Category: Bipartite]] | + | [[Category: Pedersen LC]] |
| - | [[Category: Importin]]
| + | |
| - | [[Category: Nl]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
IMA1_MOUSE Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Publication Abstract from PubMed
Despite the essential roles of pol X family enzymes in DNA repair, information about the structural basis of their nuclear import is limited. Recent studies revealed the unexpected presence of a functional nuclear localization signal (NLS) in DNA polymerase beta, indicating the importance of active nuclear targeting, even for enzymes likely to leak into and out of the nucleus. The current studies further explore the active nuclear transport of these enzymes by identifying and structurally characterizing the functional NLS sequences in the three remaining human pol X enzymes: terminal deoxynucleotidyl transferase (TdT), DNA polymerase mu (pol mu) and DNA polymerase lambda (pol lambda). NLS identifications are based on Importin alpha (Impalpha) binding affinity determined by fluorescence polarization of fluorescein-labeled NLS peptides, X-ray crystallographic analysis of the ImpalphaIBB*NLS complexes and fluorescence-based subcellular localization studies. All three polymerases use NLS sequences located near their N-terminus; TdT and pol mu utilize monopartite NLS sequences, while pol lambda utilizes a bipartite sequence, unique among the pol X family members. The pol mu NLS has relatively weak measured affinity for Impalpha, due in part to its proximity to the N-terminus that limits non-specific interactions of flanking residues preceding the NLS. However, this effect is partially mitigated by an N-terminal sequence unsupportive of Met1 removal by methionine aminopeptidase, leading to a 3-fold increase in affinity when the N-terminal methionine is present. Nuclear targeting is unique to each pol X family enzyme with variations dependent on the structure and unique functional role of each polymerase.
Variations in nuclear localization strategies among pol X family enzymes.,Kirby TW, Pedersen LC, Gabel SA, Gassman NR, London RE Traffic. 2018 Jun 22. doi: 10.1111/tra.12600. PMID:29931796[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kirby TW, Pedersen LC, Gabel SA, Gassman NR, London RE. Variations in nuclear localization strategies among pol X family enzymes. Traffic. 2018 Jun 22. doi: 10.1111/tra.12600. PMID:29931796 doi:http://dx.doi.org/10.1111/tra.12600
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