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1nlq

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[[Image:1nlq.jpg|left|200px]]
[[Image:1nlq.jpg|left|200px]]
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{{Structure
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|PDB= 1nlq |SIZE=350|CAPTION= <scene name='initialview01'>1nlq</scene>, resolution 1.50&Aring;
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|GENE= NLP OR CRP1 OR CG7917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
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{{STRUCTURE_1nlq| PDB=1nlq | SCENE= }}
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|RELATEDENTRY=[[1k5j|1K5J]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlq OCA], [http://www.ebi.ac.uk/pdbsum/1nlq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nlq RCSB]</span>
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'''The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding'''
'''The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding'''
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[[Category: Head, J F.]]
[[Category: Head, J F.]]
[[Category: Namboodiri, V M.H.]]
[[Category: Namboodiri, V M.H.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: dnlp]]
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[[Category: Dnlp]]
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[[Category: histone binding]]
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[[Category: Histone binding]]
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[[Category: nucleoplasmin]]
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[[Category: Nucleoplasmin]]
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[[Category: x-ray crystallography]]
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[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:40:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:32:07 2008''
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Revision as of 23:40, 2 May 2008

Template:STRUCTURE 1nlq

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. 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 Page seeded by OCA on Sat May 3 02:40:50 2008

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