1nlq
From Proteopedia
(Difference between revisions)
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<StructureSection load='1nlq' size='340' side='right'caption='[[1nlq]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1nlq' size='340' side='right'caption='[[1nlq]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1nlq]] is a 5 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1nlq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NLQ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1nlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlq OCA], [https://pdbe.org/1nlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nlq RCSB], [https://www.ebi.ac.uk/pdbsum/1nlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nlq ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/NLP_DROME NLP_DROME] Binds to core histones and functions in the ATP-facilitated assembly of approximately regularly spaced nucleosomal arrays. May participate in parallel with other histone-binding proteins such as NAP-1.<ref>PMID:8798787</ref> <ref>PMID:9087911</ref> Isoform 2 is inactive for chromatin assembly. In vitro it appears to form a high molecular mass aggregate with the core histones.<ref>PMID:8798787</ref> <ref>PMID:9087911</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nlq ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nlq ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The nucleoplasmin-like protein from Drosophila (dNLP) functions as a chaperone for core histones and may remodel chromatin in embryos. We now report the crystal structure of a dNLP-core pentamer at 1.5 A resolution. The monomer has an eight-stranded, beta barrel topology that is similar to nucleoplasmin (Np). However, a signature beta hairpin is tucked in along the lateral surface of the dNLP-core pentamer, while it extends outward in the Np-core decamer. Drosophila NLP and Np both assemble histone octamers. This process may require each chaperone to form a decamer, which would create symmetric binding sites for the histones. Conformational differences between dNLP and Np may reflect their different oligomeric states, while a conserved, nonpolar subunit interface may allow conformational plasticity during histone binding. | ||
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| - | The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding.,Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW Structure. 2003 Feb;11(2):175-86. PMID:12575937<ref>PMID:12575937</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1nlq" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Akey | + | [[Category: Akey CW]] |
| - | [[Category: Akey | + | [[Category: Akey IV]] |
| - | [[Category: Dutta | + | [[Category: Dutta S]] |
| - | [[Category: Head | + | [[Category: Head JF]] |
| - | [[Category: Namboodiri | + | [[Category: Namboodiri VMH]] |
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Current revision
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
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