2ayu: Difference between revisions

Latest revision as of 11:19, 22 May 2024

The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling

Structural highlights

2ayu is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Nucleosome assembly protein 1 (NAP-1) is an integral component in the establishment, maintenance, and dynamics of eukaryotic chromatin. It shuttles histones into the nucleus, assembles nucleosomes, and promotes chromatin fluidity, thereby affecting the transcription of many genes. The 3.0 A crystal structure of yeast NAP-1 reveals a previously uncharacterized fold with implications for histone binding and shuttling. A long alpha-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction. A nuclear export sequence that is embedded in the dimerization helix is almost completely masked by an accessory domain that contains several target sites for casein kinase II. The four-stranded antiparallel beta-sheet that characterizes the alpha/beta domain is found in all histone chaperones, despite the absence of homology in sequence, structural context, or quaternary structure. To our knowledge, this is the first structure of a member of the large NAP family of proteins and suggests a mechanism by which the shuttling of histones to and from the nucleus is regulated.

The structure of nucleosome assembly protein 1.,Park YJ, Luger K Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1248-53. Epub 2006 Jan 23. PMID:16432217^[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:https://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:https://dx.doi.org/MCB.01035-07
↑ Park YJ, Luger K. The structure of nucleosome assembly protein 1. Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1248-53. Epub 2006 Jan 23. PMID:16432217

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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:https://dx.doi.org/10.1091/mbc.01-10-0500

[4] 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:https://dx.doi.org/MCB.01035-07

[5] Park YJ, Luger K. The structure of nucleosome assembly protein 1. Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1248-53. Epub 2006 Jan 23. PMID:16432217

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@@ Line 3: / Line 3: @@
 <StructureSection load='2ayu' size='340' side='right'caption='[[2ayu]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ayu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AYU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ayu]] is a 1 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=2AYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AYU FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NAP1 ([https://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&#8491;</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=2ayu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayu OCA], [https://pdbe.org/2ayu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ayu RCSB], [https://www.ebi.ac.uk/pdbsum/2ayu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ayu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </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]]

2ayu: Difference between revisions

Latest revision as of 11:19, 22 May 2024

The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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