1nlq: Difference between revisions
New page: left|200px<br /><applet load="1nlq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nlq, resolution 1.50Å" /> '''The crystal structur... |
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[[Image:1nlq.jpg|left|200px]]<br /><applet load="1nlq" size=" | [[Image:1nlq.jpg|left|200px]]<br /><applet load="1nlq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nlq, resolution 1.50Å" /> | caption="1nlq, resolution 1.50Å" /> | ||
'''The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding'''<br /> | '''The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding'''<br /> | ||
==Overview== | ==Overview== | ||
The nucleoplasmin-like protein from Drosophila (dNLP) functions as a | 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. | ||
==About this Structure== | ==About this Structure== | ||
1NLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1NLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Akey, C | [[Category: Akey, C W.]] | ||
[[Category: Akey, I | [[Category: Akey, I V.]] | ||
[[Category: Dutta, S.]] | [[Category: Dutta, S.]] | ||
[[Category: Head, J | [[Category: Head, J F.]] | ||
[[Category: Namboodiri, V | [[Category: Namboodiri, V M.H.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:23 2008'' | ||
Revision as of 12:07, 21 February 2008
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The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
Overview
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.
About this Structure
1NLQ is a Single protein structure of sequence from Drosophila melanogaster with MG as ligand. Full crystallographic information is available from OCA.
Reference
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
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