1utu: Difference between revisions

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[[Image:1utu.gif|left|200px]]<br />

[[Image:1utu.gif|left|200px]]<br /><applet load="1utu" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1utu" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1utu, resolution 2.00Å" />

'''CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY TRUNCATE'''<br />

==Overview==

EMSY is a large nuclear protein that binds to the transactivation domain, of BRCA2. EMSY contains an approximately 100-residue segment at the amino, terminus called the ENT (EMSY N-terminal) domain. Plant proteins, containing ENT domains also contain members of the royal family of, chromatin-remodelling domains. It has been proposed that EMSY may have a, role in chromatin-related processes. This is supported by the observation, that a number of chromatin-regulator proteins, including HP1beta and BS69, bind directly to EMSY by means of a conserved motif adjacent to the ENT, domain. Here, we report the crystal structure of residues 1-108 of EMSY at, 2.0 A resolution. The structure contains both the ENT domain and the, HP1beta/BS69-binding motif. This binding motif forms an extended, peptide-like conformation that adopts distinct orientations in each, subunit of the dimer. Biophysical and nuclear magnetic resonance analyses, show that the main complex formed by EMSY and the chromoshadow domain of, HP1 (HP1-CSD) consists of one EMSY dimer sandwiched between two HP1-CSD, dimers. The HP1beta-binding motif is necessary and sufficient for EMSY to, bind to the chromoshadow domain of HP1beta.

EMSY is a large nuclear protein that binds to the transactivation domain of BRCA2. EMSY contains an approximately 100-residue segment at the amino terminus called the ENT (EMSY N-terminal) domain. Plant proteins containing ENT domains also contain members of the royal family of chromatin-remodelling domains. It has been proposed that EMSY may have a role in chromatin-related processes. This is supported by the observation that a number of chromatin-regulator proteins, including HP1beta and BS69, bind directly to EMSY by means of a conserved motif adjacent to the ENT domain. Here, we report the crystal structure of residues 1-108 of EMSY at 2.0 A resolution. The structure contains both the ENT domain and the HP1beta/BS69-binding motif. This binding motif forms an extended peptide-like conformation that adopts distinct orientations in each subunit of the dimer. Biophysical and nuclear magnetic resonance analyses show that the main complex formed by EMSY and the chromoshadow domain of HP1 (HP1-CSD) consists of one EMSY dimer sandwiched between two HP1-CSD dimers. The HP1beta-binding motif is necessary and sufficient for EMSY to bind to the chromoshadow domain of HP1beta.

==About this Structure==

1UTU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1UTU OCA].

1UTU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTU OCA].

==Reference==

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Line 13:

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Basu, B.P.]]

[[Category: Basu, B P.]]

[[Category: Chavali, G.B.]]

[[Category: Chavali, G B.]]

[[Category: Doherty, A.J.]]

[[Category: Doherty, A J.]]

[[Category: chromatin regulators]]

[[Category: royal family domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 19~~:38:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:16 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1utu.gif|left|200px]]<br />
+[[Image:1utu.gif|left|200px]]<br /><applet load="1utu" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1utu" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1utu, resolution 2.00&Aring;" />
 '''CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY TRUNCATE'''<br />
 ==Overview==
-EMSY is a large nuclear protein that binds to the transactivation domain, of BRCA2. EMSY contains an approximately 100-residue segment at the amino, terminus called the ENT (EMSY N-terminal) domain. Plant proteins, containing ENT domains also contain members of the royal family of, chromatin-remodelling domains. It has been proposed that EMSY may have a, role in chromatin-related processes. This is supported by the observation, that a number of chromatin-regulator proteins, including HP1beta and BS69, bind directly to EMSY by means of a conserved motif adjacent to the ENT, domain. Here, we report the crystal structure of residues 1-108 of EMSY at, 2.0 A resolution. The structure contains both the ENT domain and the, HP1beta/BS69-binding motif. This binding motif forms an extended, peptide-like conformation that adopts distinct orientations in each, subunit of the dimer. Biophysical and nuclear magnetic resonance analyses, show that the main complex formed by EMSY and the chromoshadow domain of, HP1 (HP1-CSD) consists of one EMSY dimer sandwiched between two HP1-CSD, dimers. The HP1beta-binding motif is necessary and sufficient for EMSY to, bind to the chromoshadow domain of HP1beta.
+EMSY is a large nuclear protein that binds to the transactivation domain of BRCA2. EMSY contains an approximately 100-residue segment at the amino terminus called the ENT (EMSY N-terminal) domain. Plant proteins containing ENT domains also contain members of the royal family of chromatin-remodelling domains. It has been proposed that EMSY may have a role in chromatin-related processes. This is supported by the observation that a number of chromatin-regulator proteins, including HP1beta and BS69, bind directly to EMSY by means of a conserved motif adjacent to the ENT domain. Here, we report the crystal structure of residues 1-108 of EMSY at 2.0 A resolution. The structure contains both the ENT domain and the HP1beta/BS69-binding motif. This binding motif forms an extended peptide-like conformation that adopts distinct orientations in each subunit of the dimer. Biophysical and nuclear magnetic resonance analyses show that the main complex formed by EMSY and the chromoshadow domain of HP1 (HP1-CSD) consists of one EMSY dimer sandwiched between two HP1-CSD dimers. The HP1beta-binding motif is necessary and sufficient for EMSY to bind to the chromoshadow domain of HP1beta.
 ==About this Structure==
-UTU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UTU OCA].
+UTU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTU OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Basu, B.P.]]
+[[Category: Basu, B P.]]
-[[Category: Chavali, G.B.]]
+[[Category: Chavali, G B.]]
-[[Category: Doherty, A.J.]]
+[[Category: Doherty, A J.]]
 [[Category: chromatin regulators]]
 [[Category: royal family domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:38:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:16 2008''