1zx2

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[[Image:1zx2.gif|left|200px]]
[[Image:1zx2.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1zx2", creates the "Structure Box" on the page.
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|GENE= BRE5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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{{STRUCTURE_1zx2| PDB=1zx2 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zx2 OCA], [http://www.ebi.ac.uk/pdbsum/1zx2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zx2 RCSB]</span>
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'''Crystal Structure of Yeast UBP3-associated Protein BRE5'''
'''Crystal Structure of Yeast UBP3-associated Protein BRE5'''
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[[Category: Ossareh-Nazari, B.]]
[[Category: Ossareh-Nazari, B.]]
[[Category: Zhao, K.]]
[[Category: Zhao, K.]]
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[[Category: deubiqutinate]]
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[[Category: Deubiqutinate]]
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[[Category: ntf2]]
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[[Category: Ntf2]]
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[[Category: ubp3]]
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[[Category: Ubp3]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:11:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:42:45 2008''
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Revision as of 15:11, 3 May 2008

Template:STRUCTURE 1zx2

Crystal Structure of Yeast UBP3-associated Protein BRE5


Overview

The Bre5 protein is a cofactor for the deubiquitinating enzyme Ubp3, and it contains a nuclear transfer factor 2 (NTF2)-like protein recognition module that is essential for Ubp3 activity. In this study, we report the x-ray crystal structure of the Bre5 NTF2-like domain and show that it forms a homodimeric structure that is similar to other NTF2-like domains, except for the presence of an intermolecular disulfide bond in the crystals. Sedimentation equilibrium studies reveal that under non-reducing conditions, the Bre5 NTF2-like domain is exclusively dimeric, whereas a disulfide bond-deficient mutant undergoes a monomer-dimer equilibrium with a dissociation constant in the midnanomolar range, suggesting that dimer formation and possibly also disulfide bond formation may modulate Bre5 function in vivo. Using deletion analysis, we also identify a novel N-terminal domain of Ubp3 that is necessary and sufficient for interaction with Bre5 and use isothermal titration calorimetry to show that Bre5 and Ubp3 form a 2:1 complex, in contrast to other reported NTF2-like domain/protein interactions that form 1:1 complexes. Finally, we employ structure-based mutagenesis to map the Ubp3 binding surface of Bre5 to a region near the Bre5 dimer interface and show that this binding surface of Bre5 is important for Ubp3 function in vivo. Together, these studies provide novel insights into protein recognition by NTF2-like domains and provide a molecular scaffold for understanding how Ubp3 function is regulated by Bre5 cofactor binding.

About this Structure

1ZX2 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for interaction between the Ubp3 deubiquitinating enzyme and its Bre5 cofactor., Li K, Zhao K, Ossareh-Nazari B, Da G, Dargemont C, Marmorstein R, J Biol Chem. 2005 Aug 12;280(32):29176-85. Epub 2005 Jun 13. PMID:15955808 Page seeded by OCA on Sat May 3 18:11:04 2008

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