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| | ==Nucleosome assembly proteins I (NAP-1, 74-365)== | | ==Nucleosome assembly proteins I (NAP-1, 74-365)== |
| - | <StructureSection load='2z2r' size='340' side='right' caption='[[2z2r]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='2z2r' size='340' side='right'caption='[[2z2r]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2z2r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z2R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2z2r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z2R FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</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=2z2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2r OCA], [http://pdbe.org/2z2r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z2r RCSB], [http://www.ebi.ac.uk/pdbsum/2z2r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2r ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2r OCA], [https://pdbe.org/2z2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z2r RCSB], [https://www.ebi.ac.uk/pdbsum/2z2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAP1_YEAST NAP1_YEAST]] Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.<ref>PMID:2016313</ref> <ref>PMID:7622566</ref> <ref>PMID:12058072</ref> <ref>PMID:18086883</ref> | + | [https://www.uniprot.org/uniprot/NAP1_YEAST NAP1_YEAST] Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.<ref>PMID:2016313</ref> <ref>PMID:7622566</ref> <ref>PMID:12058072</ref> <ref>PMID:18086883</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/2z2r_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/2z2r_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Luger, K]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Park, Y J]] | + | [[Category: Luger K]] |
| - | [[Category: Chaperone]] | + | [[Category: Park YJ]] |
| - | [[Category: Histone chaperone]]
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| Structural highlights
Function
NAP1_YEAST Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.[1] [2] [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 histone chaperone nucleosome assembly protein 1 (NAP1) is implicated in histone shuttling as well as nucleosome assembly and disassembly. Under physiological conditions, NAP1 dimers exist in a mixture of various high-molecular-weight oligomers whose size may be regulated by the cell cycle-dependent concentration of NAP1. Both the functional and structural significance of the observed oligomers are unknown. We have resolved the molecular mechanism by which yeast NAP1 (yNAP1) dimers oligomerize by applying x-ray crystallographic, hydrodynamic, and functional approaches. We found that an extended beta-hairpin that protrudes from the compact core of the yNAP1 dimer forms a stable beta-sheet with beta-hairpins of neighboring yNAP1 dimers. Disruption of the beta-hairpin (whose sequence is conserved among NAP1 proteins in various species) by the replacement of one or more amino acids with proline results in complete loss of yNAP1 dimer oligomerization. The in vitro functions of yNAP1 remain unaffected by the mutations. We have thus identified a conserved structural feature of NAP1 whose function, in addition to presenting the nuclear localization sequence, appears to be the formation of higher-order oligomers.
A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1.,Park YJ, McBryant SJ, Luger K J Mol Biol. 2008 Jan 25;375(4):1076-85. Epub 2007 Nov 19. PMID:18068721[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ishimi Y, Kikuchi A. Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J Biol Chem. 1991 Apr 15;266(11):7025-9. PMID:2016313
- ↑ Kellogg DR, Kikuchi A, Fujii-Nakata T, Turck CW, Murray AW. Members of the NAP/SET family of proteins interact specifically with B-type cyclins. J Cell Biol. 1995 Aug;130(3):661-73. PMID:7622566
- ↑ Mortensen EM, McDonald H, Yates J 3rd, Kellogg DR. Cell cycle-dependent assembly of a Gin4-septin complex. Mol Biol Cell. 2002 Jun;13(6):2091-105. PMID:12058072 doi:http://dx.doi.org/10.1091/mbc.01-10-0500
- ↑ Calvert ME, Keck KM, Ptak C, Shabanowitz J, Hunt DF, Pemberton LF. Phosphorylation by casein kinase 2 regulates Nap1 localization and function. Mol Cell Biol. 2008 Feb;28(4):1313-25. Epub 2007 Dec 17. PMID:18086883 doi:http://dx.doi.org/MCB.01035-07
- ↑ Park YJ, McBryant SJ, Luger K. A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1. J Mol Biol. 2008 Jan 25;375(4):1076-85. Epub 2007 Nov 19. PMID:18068721 doi:10.1016/j.jmb.2007.11.031
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