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| | <StructureSection load='6j2z' size='340' side='right'caption='[[6j2z]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='6j2z' size='340' side='right'caption='[[6j2z]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j2z]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J2Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j2z]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J2Z FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6j2m|6j2m]]</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP53, At4g25340, T30C3_20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=6j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j2z OCA], [https://pdbe.org/6j2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j2z RCSB], [https://www.ebi.ac.uk/pdbsum/6j2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j2z ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j2z OCA], [http://pdbe.org/6j2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j2z RCSB], [http://www.ebi.ac.uk/pdbsum/6j2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j2z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FKB53_ARATH FKB53_ARATH] |
| | <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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Singh AK]] |
| - | [[Category: Singh, A K]] | + | [[Category: Vasudevan D]] |
| - | [[Category: Vasudevan, D]] | + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Fkbp]]
| + | |
| - | [[Category: Fkbp-nucleoplasmin]]
| + | |
| - | [[Category: Histone chaperone]]
| + | |
| Structural highlights
Function
FKB53_ARATH
Publication Abstract from PubMed
FKBP53 is one of the seven multi-domain FK506-binding proteins present in Arabidopsis thaliana, and it is known to get targeted to the nucleus. It has a conserved PPIase domain at the C-terminus and a highly charged N-terminal stretch, which has been reported to bind to histone H3 and perform the function of a histone chaperone. To better understand the molecular details of this PPIase with histone chaperoning activity, we have solved the crystal structures of its terminal domains and functionally characterized them. The C-terminal domain showed strong PPIase activity, no role in histone chaperoning and revealed a monomeric five-beta palm-like fold that wrapped over a helix, typical of an FK506-binding domain. The N-terminal domain had a pentameric nucleoplasmin-fold; making this the first report of a plant nucleoplasmin structure. Further characterization revealed the N-terminal nucleoplasmin domain to interact with H2A/H2B and H3/H4 histone oligomers, individually, as well as simultaneously, suggesting two different binding sites for H2A/H2B and H3/H4. The pentameric domain assists nucleosome assembly and forms a discrete complex with pre-formed nucleosomes; wherein two pentamers bind to a nucleosome.
AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.,Singh AK, Datta A, Jobichen C, Luan S, Vasudevan D Nucleic Acids Res. 2019 Dec 6. pii: 5661091. doi: 10.1093/nar/gkz1153. PMID:31807785[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singh AK, Datta A, Jobichen C, Luan S, Vasudevan D. AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains. Nucleic Acids Res. 2019 Dec 6. pii: 5661091. doi: 10.1093/nar/gkz1153. PMID:31807785 doi:http://dx.doi.org/10.1093/nar/gkz1153
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