2fid: Difference between revisions

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New page: left|200px<br /><applet load="2fid" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fid, resolution 2.80Å" /> '''Crystal Structure of...
 
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[[Image:2fid.gif|left|200px]]<br /><applet load="2fid" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2fid.gif|left|200px]]<br /><applet load="2fid" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2fid, resolution 2.80&Aring;" />
caption="2fid, resolution 2.80&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==
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.
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==
2FID 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FID OCA].  
2FID 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FID OCA].  


==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Hurley, J.H.]]
[[Category: Hurley, J H.]]
[[Category: Lee, S.]]
[[Category: Lee, S.]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc finger]]
[[Category: zinc finger]]


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Revision as of 18:21, 21 February 2008

File:2fid.gif


2fid, resolution 2.80Å

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

OverviewOverview

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 StructureAbout this Structure

2FID is a Protein complex structure of sequences from Bos taurus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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