2ayu: Difference between revisions

Revision as of 17:32, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

2AYU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:32:25 2008

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OCA

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-[[Image:2ayu.gif|left|200px]]<br /><applet load="2ayu" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="2ayu, resolution 3.&Aring;" />
 '''The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-AYU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AYU OCA].
+AYU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Luger, K.]]
-[[Category: Park, Y.J.]]
+[[Category: Park, Y J.]]
 [[Category: histone chaperone]]
 [[Category: nucleosome assembly protein 1 (nap1)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:28:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:25 2008''