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1nlq

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Revision as of 08:03, 25 December 2014

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding

Structural highlights

1nlq is a 5 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1k5j
Gene:	NLP OR CRP1 OR CG7917 (Drosophila melanogaster)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] Isoform 2 is inactive for chromatin assembly. In vitro it appears to form a high molecular mass aggregate with the core histones.^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ito T, Tyler JK, Bulger M, Kobayashi R, Kadonaga JT. ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. J Biol Chem. 1996 Oct 4;271(40):25041-8. PMID:8798787
↑ Crevel G, Huikeshoven H, Cotterill S, Simon M, Wall J, Philpott A, Laskey RA, McConnell M, Fisher PA, Berrios M. Molecular and cellular characterization of CRP1, a Drosophila chromatin decondensation protein. J Struct Biol. 1997 Feb;118(1):9-22. PMID:9087911 doi:http://dx.doi.org/S1047-8477(96)93836-8
↑ Ito T, Tyler JK, Bulger M, Kobayashi R, Kadonaga JT. ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. J Biol Chem. 1996 Oct 4;271(40):25041-8. PMID:8798787
↑ Crevel G, Huikeshoven H, Cotterill S, Simon M, Wall J, Philpott A, Laskey RA, McConnell M, Fisher PA, Berrios M. Molecular and cellular characterization of CRP1, a Drosophila chromatin decondensation protein. J Struct Biol. 1997 Feb;118(1):9-22. PMID:9087911 doi:http://dx.doi.org/S1047-8477(96)93836-8
↑ Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW. The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding. Structure. 2003 Feb;11(2):175-86. PMID:12575937

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nlq"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1nlq]] is a 5 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NLQ FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k5j|1k5j]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k5j|1k5j]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NLP OR CRP1 OR CG7917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NLP OR CRP1 OR CG7917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1nlq RCSB], [http://www.ebi.ac.uk/pdbsum/1nlq PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1nlq RCSB], [http://www.ebi.ac.uk/pdbsum/1nlq PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Drosophila melanogaster]]
-[[Category: Akey, C W.]]
+[[Category: Akey, C W]]
-[[Category: Akey, I V.]]
+[[Category: Akey, I V]]
-[[Category: Dutta, S.]]
+[[Category: Dutta, S]]
-[[Category: Head, J F.]]
+[[Category: Head, J F]]
-[[Category: Namboodiri, V M.H.]]
+[[Category: Namboodiri, V M.H]]
 [[Category: Chaperone]]
 [[Category: Dnlp]]

1nlq

From Proteopedia

Revision as of 08:03, 25 December 2014

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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