|
|
| (11 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:1nlq.jpg|left|200px]] | |
| | | | |
| - | {{Structure
| + | ==The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding== |
| - | |PDB= 1nlq |SIZE=350|CAPTION= <scene name='initialview01'>1nlq</scene>, resolution 1.50Å
| + | <StructureSection load='1nlq' size='340' side='right'caption='[[1nlq]], [[Resolution|resolution]] 1.50Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
| + | <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> |
| - | |ACTIVITY=
| + | </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> |
| - | |GENE= NLP OR CRP1 OR CG7917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
| + | <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> |
| - | |DOMAIN=
| + | <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> |
| - | |RELATEDENTRY=[[1k5j|1K5J]]
| + | </table> |
| - | |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>
| + | == 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 == |
| - | '''The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | | + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nlq_consurf.spt"</scriptWhenChecked> |
| - | 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.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 1NLQ is a [[Single protein]] structure of 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].
| + | </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> |
| - | ==Reference== | + | == References == |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12575937 12575937]
| + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Drosophila melanogaster]] | | [[Category: Drosophila melanogaster]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Akey, C W.]] | + | [[Category: Akey CW]] |
| - | [[Category: Akey, I V.]] | + | [[Category: Akey IV]] |
| - | [[Category: Dutta, S.]] | + | [[Category: Dutta S]] |
| - | [[Category: Head, J F.]] | + | [[Category: Head JF]] |
| - | [[Category: Namboodiri, V M.H.]] | + | [[Category: Namboodiri VMH]] |
| - | [[Category: chaperone]]
| + | |
| - | [[Category: dnlp]]
| + | |
| - | [[Category: histone binding]]
| + | |
| - | [[Category: nucleoplasmin]]
| + | |
| - | [[Category: x-ray crystallography]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:32:07 2008''
| + | |
| Structural highlights
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.
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
|
