2fif

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(New page: 200px<br /><applet load="2fif" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fif, resolution 2.49&Aring;" /> '''Crystal Structure of...)
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[[Image:2fif.gif|left|200px]]<br /><applet load="2fif" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fif.gif|left|200px]]<br /><applet load="2fif" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fif, resolution 2.49&Aring;" />
caption="2fif, resolution 2.49&Aring;" />
'''Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin'''<br />
'''Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin'''<br />
==Overview==
==Overview==
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Rabex-5 is an exchange factor for Rab5, a master regulator of endosomal, trafficking. Rabex-5 binds monoubiquitin, undergoes covalent, ubiquitination and contains an intrinsic ubiquitin ligase activity, all of, which require an N-terminal A20 zinc finger followed immediately by a, helix. The structure of the N-terminal portion of Rabex-5 bound to, ubiquitin at 2.5-A resolution shows that Rabex-5-ubiquitin interactions, occur at two sites. The first site is a new type of ubiquitin-binding, domain, an inverted ubiquitin-interacting motif, which binds with, approximately 29-microM affinity to the canonical Ile44 hydrophobic patch, on ubiquitin. The second is a diaromatic patch on the A20 zinc finger, which binds with approximately 22-microM affinity to a polar region, centered on Asp58 of ubiquitin. The A20 zinc-finger diaromatic patch, mediates ubiquitin-ligase activity by directly recruiting a, ubiquitin-loaded ubiquitin-conjugating enzyme.
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Rabex-5 is an exchange factor for Rab5, a master regulator of endosomal trafficking. Rabex-5 binds monoubiquitin, undergoes covalent ubiquitination and contains an intrinsic ubiquitin ligase activity, all of which require an N-terminal A20 zinc finger followed immediately by a helix. The structure of the N-terminal portion of Rabex-5 bound to ubiquitin at 2.5-A resolution shows that Rabex-5-ubiquitin interactions occur at two sites. The first site is a new type of ubiquitin-binding domain, an inverted ubiquitin-interacting motif, which binds with approximately 29-microM affinity to the canonical Ile44 hydrophobic patch on ubiquitin. The second is a diaromatic patch on the A20 zinc finger, which binds with approximately 22-microM affinity to a polar region centered on Asp58 of ubiquitin. The A20 zinc-finger diaromatic patch mediates ubiquitin-ligase activity by directly recruiting a ubiquitin-loaded ubiquitin-conjugating enzyme.
==About this Structure==
==About this Structure==
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2FIF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FIF OCA].
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2FIF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FIF OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: Lee, S.]]
[[Category: Lee, S.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:34:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:42 2008''

Revision as of 15:21, 21 February 2008


2fif, resolution 2.49Å

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Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin

Overview

Rabex-5 is an exchange factor for Rab5, a master regulator of endosomal trafficking. Rabex-5 binds monoubiquitin, undergoes covalent ubiquitination and contains an intrinsic ubiquitin ligase activity, all of which require an N-terminal A20 zinc finger followed immediately by a helix. The structure of the N-terminal portion of Rabex-5 bound to ubiquitin at 2.5-A resolution shows that Rabex-5-ubiquitin interactions occur at two sites. The first site is a new type of ubiquitin-binding domain, an inverted ubiquitin-interacting motif, which binds with approximately 29-microM affinity to the canonical Ile44 hydrophobic patch on ubiquitin. The second is a diaromatic patch on the A20 zinc finger, which binds with approximately 22-microM affinity to a polar region centered on Asp58 of ubiquitin. The A20 zinc-finger diaromatic patch mediates ubiquitin-ligase activity by directly recruiting a ubiquitin-loaded ubiquitin-conjugating enzyme.

About this Structure

2FIF is a Protein complex structure of sequences from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5., Lee S, Tsai YC, Mattera R, Smith WJ, Kostelansky MS, Weissman AM, Bonifacino JS, Hurley JH, Nat Struct Mol Biol. 2006 Mar;13(3):264-71. Epub 2006 Feb 5. PMID:16462746

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