4ca9: Difference between revisions
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==Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39== | ==Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39== | ||
<StructureSection load='4ca9' size='340' side='right' caption='[[4ca9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='4ca9' size='340' side='right' caption='[[4ca9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[4ca9]] is a 5 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CA9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ca9]] is a 5 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CA9 FirstGlance]. <br> | ||
</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> | </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=4ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ca9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ca9 PDBsum]</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=4ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ca9 OCA], [http://pdbe.org/4ca9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ca9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ca9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | |||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FKB39_DROME FKB39_DROME]] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. | [[http://www.uniprot.org/uniprot/FKB39_DROME FKB39_DROME]] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ca9" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 20:28, 9 March 2017
Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Function[FKB39_DROME] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. Publication Abstract from PubMedNucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals. The Pentameric Nucleoplasmin Fold Is Present in Drosophila FKBP39 and a Large Number of Chromatin-Related Proteins.,Edlich-Muth C, Artero JB, Callow P, Przewloka MR, Watson AA, Zhang W, Glover DM, Debski J, Dadlez M, Round AR, Forsyth VT, Laue ED J Mol Biol. 2015 Mar 24. pii: S0022-2836(15)00194-1. doi:, 10.1016/j.jmb.2015.03.010. PMID:25813344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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