1wrd: Difference between revisions

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

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

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

caption="1wrd, resolution 1.75Å" />

'''Crystal structure of Tom1 GAT domain in complex with ubiquitin'''<br />

==Overview==

Tom1 (Target of Myb1) is suggested to be involved in the transport of, ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1), domain with ubiquitin. Here, we demonstrate that the three-helix bundle of, Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44, surface of ubiquitin. The complex crystal structure demonstrates that the, first site is a hydrophobic patch on helices alpha1 and alpha2. NMR and, biochemical data revealed that the N-terminal half of helix alpha3 of, Tom1-GAT constitutes the second, stronger binding site. The double-sided, ubiquitin binding enhances the efficiency of recognition of ubiquitinated, proteins by Tom1.

Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices alpha1 and alpha2. NMR and biochemical data revealed that the N-terminal half of helix alpha3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.

==About this Structure==

1WRD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WRD OCA].

1WRD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRD OCA].

==Reference==

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[[Category: ubiquitin-binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 19~~:54:~~00 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:20 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1wrd.gif|left|200px]]<br />
+[[Image:1wrd.gif|left|200px]]<br /><applet load="1wrd" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1wrd" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1wrd, resolution 1.75&Aring;" />
 '''Crystal structure of Tom1 GAT domain in complex with ubiquitin'''<br />
 ==Overview==
-Tom1 (Target of Myb1) is suggested to be involved in the transport of, ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1), domain with ubiquitin. Here, we demonstrate that the three-helix bundle of, Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44, surface of ubiquitin. The complex crystal structure demonstrates that the, first site is a hydrophobic patch on helices alpha1 and alpha2. NMR and, biochemical data revealed that the N-terminal half of helix alpha3 of, Tom1-GAT constitutes the second, stronger binding site. The double-sided, ubiquitin binding enhances the efficiency of recognition of ubiquitinated, proteins by Tom1.
+Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices alpha1 and alpha2. NMR and biochemical data revealed that the N-terminal half of helix alpha3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.
 ==About this Structure==
-WRD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WRD OCA].
+WRD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRD OCA].
 ==Reference==
@@ Line 27: / Line 26: @@
 [[Category: ubiquitin-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:54:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:20 2008''