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1nlq
From Proteopedia
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|PDB= 1nlq |SIZE=350|CAPTION= <scene name='initialview01'>1nlq</scene>, resolution 1.50Å | |PDB= 1nlq |SIZE=350|CAPTION= <scene name='initialview01'>1nlq</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NLP OR CRP1 OR CG7917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | |GENE= NLP OR CRP1 OR CG7917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k5j|1K5J]] | ||
| + | |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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[[Category: Head, J F.]] | [[Category: Head, J F.]] | ||
[[Category: Namboodiri, V M.H.]] | [[Category: Namboodiri, V M.H.]] | ||
| - | [[Category: MG]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: dnlp]] | [[Category: dnlp]] | ||
| Line 34: | Line 36: | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:32:07 2008'' |
Revision as of 19:32, 30 March 2008
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | NLP OR CRP1 OR CG7917 (Drosophila melanogaster) | ||||||
| Related: | 1K5J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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