2e50
From Proteopedia
(New page: 200px<br /> <applet load="2e50" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e50, resolution 2.30Å" /> '''Crystal structure o...) |
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caption="2e50, resolution 2.30Å" /> | caption="2e50, resolution 2.30Å" /> | ||
'''Crystal structure of SET/TAF-1beta/INHAT'''<br /> | '''Crystal structure of SET/TAF-1beta/INHAT'''<br /> | ||
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==Overview== | ==Overview== | ||
Histone chaperones assemble and disassemble nucleosomes in an, ATP-independent manner and thus regulate the most fundamental step in the, alteration of chromatin structure. The molecular mechanisms underlying, histone chaperone activity remain unclear. To gain insights into these, mechanisms, we solved the crystal structure of the functional domain of, SET/TAF-Ibeta/INHAT at a resolution of 2.3 A. We found that, SET/TAF-Ibeta/INHAT formed a dimer that assumed a "headphone"-like, structure. Each subunit of the SET/TAF-Ibeta/INHAT dimer consisted of an N, terminus, a backbone helix, and an "earmuff" domain. It resembles the, structure of the related protein NAP-1. Comparison of the crystal, structures of SET/TAF-Ibeta/INHAT and NAP-1 revealed that the two proteins, were folded similarly except for an inserted helix. However, their, backbone helices were shaped differently, and the relative dispositions of, the backbone helix and the earmuff domain between the two proteins, differed by approximately 40 degrees . Our biochemical analyses of mutants, revealed that the region of SET/TAF-Ibeta/INHAT that is engaged in histone, chaperone activity is the bottom surface of the earmuff domain, because, this surface bound both core histones and double-stranded DNA. This, overlap or closeness of the activity surface and the binding surfaces, suggests that the specific association among SET/TAF-Ibeta/INHAT, core, histones, and double-stranded DNA is requisite for histone chaperone, activity. These findings provide insights into the possible mechanisms by, which histone chaperones assemble and disassemble nucleosome structures. | Histone chaperones assemble and disassemble nucleosomes in an, ATP-independent manner and thus regulate the most fundamental step in the, alteration of chromatin structure. The molecular mechanisms underlying, histone chaperone activity remain unclear. To gain insights into these, mechanisms, we solved the crystal structure of the functional domain of, SET/TAF-Ibeta/INHAT at a resolution of 2.3 A. We found that, SET/TAF-Ibeta/INHAT formed a dimer that assumed a "headphone"-like, structure. Each subunit of the SET/TAF-Ibeta/INHAT dimer consisted of an N, terminus, a backbone helix, and an "earmuff" domain. It resembles the, structure of the related protein NAP-1. Comparison of the crystal, structures of SET/TAF-Ibeta/INHAT and NAP-1 revealed that the two proteins, were folded similarly except for an inserted helix. However, their, backbone helices were shaped differently, and the relative dispositions of, the backbone helix and the earmuff domain between the two proteins, differed by approximately 40 degrees . Our biochemical analyses of mutants, revealed that the region of SET/TAF-Ibeta/INHAT that is engaged in histone, chaperone activity is the bottom surface of the earmuff domain, because, this surface bound both core histones and double-stranded DNA. This, overlap or closeness of the activity surface and the binding surfaces, suggests that the specific association among SET/TAF-Ibeta/INHAT, core, histones, and double-stranded DNA is requisite for histone chaperone, activity. These findings provide insights into the possible mechanisms by, which histone chaperones assemble and disassemble nucleosome structures. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Leukemia, acute T-cell lymphoblastic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611060 611060]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2E50 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with TRE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2E50 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=TRE:'>TRE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E50 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: set]] | [[Category: set]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:02:59 2008'' |
Revision as of 13:03, 23 January 2008
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Crystal structure of SET/TAF-1beta/INHAT
Overview
Histone chaperones assemble and disassemble nucleosomes in an, ATP-independent manner and thus regulate the most fundamental step in the, alteration of chromatin structure. The molecular mechanisms underlying, histone chaperone activity remain unclear. To gain insights into these, mechanisms, we solved the crystal structure of the functional domain of, SET/TAF-Ibeta/INHAT at a resolution of 2.3 A. We found that, SET/TAF-Ibeta/INHAT formed a dimer that assumed a "headphone"-like, structure. Each subunit of the SET/TAF-Ibeta/INHAT dimer consisted of an N, terminus, a backbone helix, and an "earmuff" domain. It resembles the, structure of the related protein NAP-1. Comparison of the crystal, structures of SET/TAF-Ibeta/INHAT and NAP-1 revealed that the two proteins, were folded similarly except for an inserted helix. However, their, backbone helices were shaped differently, and the relative dispositions of, the backbone helix and the earmuff domain between the two proteins, differed by approximately 40 degrees . Our biochemical analyses of mutants, revealed that the region of SET/TAF-Ibeta/INHAT that is engaged in histone, chaperone activity is the bottom surface of the earmuff domain, because, this surface bound both core histones and double-stranded DNA. This, overlap or closeness of the activity surface and the binding surfaces, suggests that the specific association among SET/TAF-Ibeta/INHAT, core, histones, and double-stranded DNA is requisite for histone chaperone, activity. These findings provide insights into the possible mechanisms by, which histone chaperones assemble and disassemble nucleosome structures.
About this Structure
2E50 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity., Muto S, Senda M, Akai Y, Sato L, Suzuki T, Nagai R, Senda T, Horikoshi M, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4285-90. Epub 2007 Mar 6. PMID:17360516
Page seeded by OCA on Wed Jan 23 15:02:59 2008
Categories: Homo sapiens | Single protein | Horikoshi, M. | Muto, S. | Senda, M. | Senda, T. | TRE | Histone chaperone | Inhat | Pp2ai | Set
