3t30

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Current revision (13:16, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3t30' size='340' side='right'caption='[[3t30]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3t30' size='340' side='right'caption='[[3t30]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t30]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T30 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t30]] is a 10 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=3T30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T30 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NPM2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=3t30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t30 OCA], [https://pdbe.org/3t30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t30 RCSB], [https://www.ebi.ac.uk/pdbsum/3t30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t30 ProSAT]</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=3t30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t30 OCA], [https://pdbe.org/3t30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t30 RCSB], [https://www.ebi.ac.uk/pdbsum/3t30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t30 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NPM2_HUMAN NPM2_HUMAN]] Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization.<ref>PMID:21863821</ref>
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[https://www.uniprot.org/uniprot/NPM2_HUMAN NPM2_HUMAN] Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization.<ref>PMID:21863821</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human Npm2 is an ortholog of Xenopus nucleoplasmin (Np), a chaperone that binds histones. We have determined the crystal structure of a truncated Npm2-core at 1.9 A resolution and show that the N-terminal domains of Npm2 and Np form similar pentamers. This allowed us to model an Npm2 decamer which may be formed by hydrogen bonds between quasi-conserved residues in the interface between two pentamers. Interestingly, the Npm2 pentamer lacks a prototypical A1-acidic tract in each of its subunits. This feature may be responsible for the inability of Npm2-core to bind histones. However, Npm2 with a large acidic tract in its C-terminal tail (Npm2-A2) is able to bind histones and form large complexes. Fluorescence resonance energy transfer experiments and biochemical analysis of loop mutations support the premise that nucleoplasmins form decamers when they bind H2A-H2B dimers and H3-H4 tetramers simultaneously. In the absence of histone tetramers, these chaperones bind H2A-H2B dimers with a single pentamer forming the central hub. When taken together, our data provide insights into the mechanism of histone binding by nucleoplasmins.
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Crystal Structure and Function of Human Nucleoplasmin (Npm2): A Histone Chaperone in Oocytes and Embryos.,Platonova O, Akey IV, Head JF, Akey CW Biochemistry. 2011 Sep 20;50(37):8078-8089. Epub 2011 Aug 24. PMID:21863821<ref>PMID:21863821</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t30" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Akey, C W]]
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[[Category: Akey CW]]
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[[Category: Head, J F]]
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[[Category: Head JF]]
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[[Category: Platonova, O]]
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[[Category: Platonova O]]
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[[Category: Beta-barrel jelly roll topology]]
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[[Category: Chaperone]]
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[[Category: H2a-h2b dimer and h3-h4 tetramer]]
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[[Category: Histone chaperone]]
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[[Category: Oocytes and early embryo]]
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Current revision

Human nucleoplasmin (Npm2): a histone chaperone in oocytes and early embryos

PDB ID 3t30

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