1ukx: Difference between revisions

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[[Image:1ukx.jpg|left|200px]]<br /><applet load="1ukx" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

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

caption="1ukx" />

'''Solution structure of the RWD domain of mouse GCN2'''<br />

==Overview==

GCN2 is the alpha-subunit of the only translation initiation factor, (eIF2alpha) kinase that appears in all eukaryotes. Its function requires, an interaction with GCN1 via the domain at its N-terminus, which is termed, the RWD domain after three major RWD-containing proteins: RING, finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD, (DEXD)-like helicases. In this study, we determined the solution structure, of the mouse GCN2 RWD domain using NMR spectroscopy. The structure forms, an alpha + beta sandwich fold consisting of two layers: a four-stranded, antiparallel beta-sheet, and three side-by-side alpha-helices, with an, alphabetabetabetabetaalphaalpha topology. A characteristic YPXXXP motif, which always occurs in RWD domains, forms a stable loop including three, consecutive beta-turns that overlap with each other by two residues, (triple beta-turn). As putative binding sites with GCN1, a structure-based, alignment allowed the identification of several surface residues in, alpha-helix 3 that are characteristic of the GCN2 RWD domains. Despite the, apparent absence of sequence similarity, the RWD structure significantly, resembles that of ubiquitin-conjugating enzymes (E2s), with most of the, structural differences in the region connecting beta-strand 4 and, alpha-helix 3. The structural architecture, including the triple, beta-turn, is fundamentally common among various RWD domains and E2s, but, most of the surface residues on the structure vary. Thus, it appears that, the RWD domain is a novel structural domain for protein-binding that plays, specific roles in individual RWD-containing proteins.

GCN2 is the alpha-subunit of the only translation initiation factor (eIF2alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. In this study, we determined the solution structure of the mouse GCN2 RWD domain using NMR spectroscopy. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices, with an alphabetabetabetabetaalphaalpha topology. A characteristic YPXXXP motif, which always occurs in RWD domains, forms a stable loop including three consecutive beta-turns that overlap with each other by two residues (triple beta-turn). As putative binding sites with GCN1, a structure-based alignment allowed the identification of several surface residues in alpha-helix 3 that are characteristic of the GCN2 RWD domains. Despite the apparent absence of sequence similarity, the RWD structure significantly resembles that of ubiquitin-conjugating enzymes (E2s), with most of the structural differences in the region connecting beta-strand 4 and alpha-helix 3. The structural architecture, including the triple beta-turn, is fundamentally common among various RWD domains and E2s, but most of the surface residues on the structure vary. Thus, it appears that the RWD domain is a novel structural domain for protein-binding that plays specific roles in individual RWD-containing proteins.

==About this Structure==

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

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

==Reference==

Line 17:

[[Category: Koshiba, S.]]

[[Category: Nameki, N.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Yokoyama, S.]]

[[Category: Yoneyama, M.]]

Line 27:

[[Category: ubc-like fold]]

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@@ Line 1: / Line 1: @@
-[[Image:1ukx.jpg|left|200px]]<br /><applet load="1ukx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ukx.jpg|left|200px]]<br /><applet load="1ukx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ukx" />
 '''Solution structure of the RWD domain of mouse GCN2'''<br />
 ==Overview==
-GCN2 is the alpha-subunit of the only translation initiation factor, (eIF2alpha) kinase that appears in all eukaryotes. Its function requires, an interaction with GCN1 via the domain at its N-terminus, which is termed, the RWD domain after three major RWD-containing proteins: RING, finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD, (DEXD)-like helicases. In this study, we determined the solution structure, of the mouse GCN2 RWD domain using NMR spectroscopy. The structure forms, an alpha + beta sandwich fold consisting of two layers: a four-stranded, antiparallel beta-sheet, and three side-by-side alpha-helices, with an, alphabetabetabetabetaalphaalpha topology. A characteristic YPXXXP motif, which always occurs in RWD domains, forms a stable loop including three, consecutive beta-turns that overlap with each other by two residues, (triple beta-turn). As putative binding sites with GCN1, a structure-based, alignment allowed the identification of several surface residues in, alpha-helix 3 that are characteristic of the GCN2 RWD domains. Despite the, apparent absence of sequence similarity, the RWD structure significantly, resembles that of ubiquitin-conjugating enzymes (E2s), with most of the, structural differences in the region connecting beta-strand 4 and, alpha-helix 3. The structural architecture, including the triple, beta-turn, is fundamentally common among various RWD domains and E2s, but, most of the surface residues on the structure vary. Thus, it appears that, the RWD domain is a novel structural domain for protein-binding that plays, specific roles in individual RWD-containing proteins.
+GCN2 is the alpha-subunit of the only translation initiation factor (eIF2alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. In this study, we determined the solution structure of the mouse GCN2 RWD domain using NMR spectroscopy. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices, with an alphabetabetabetabetaalphaalpha topology. A characteristic YPXXXP motif, which always occurs in RWD domains, forms a stable loop including three consecutive beta-turns that overlap with each other by two residues (triple beta-turn). As putative binding sites with GCN1, a structure-based alignment allowed the identification of several surface residues in alpha-helix 3 that are characteristic of the GCN2 RWD domains. Despite the apparent absence of sequence similarity, the RWD structure significantly resembles that of ubiquitin-conjugating enzymes (E2s), with most of the structural differences in the region connecting beta-strand 4 and alpha-helix 3. The structural architecture, including the triple beta-turn, is fundamentally common among various RWD domains and E2s, but most of the surface residues on the structure vary. Thus, it appears that the RWD domain is a novel structural domain for protein-binding that plays specific roles in individual RWD-containing proteins.
 ==About this Structure==
-UKX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UKX OCA].
+UKX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UKX OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Koshiba, S.]]
 [[Category: Nameki, N.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Yokoyama, S.]]
 [[Category: Yoneyama, M.]]
@@ Line 27: / Line 27: @@
 [[Category: ubc-like fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:12:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:44 2008''