1nb8

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|PDB= 1nb8 |SIZE=350|CAPTION= <scene name='initialview01'>1nb8</scene>, resolution 2.3&Aring;
|PDB= 1nb8 |SIZE=350|CAPTION= <scene name='initialview01'>1nb8</scene>, resolution 2.3&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </span>
|GENE= USP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= USP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nb8 OCA], [http://www.ebi.ac.uk/pdbsum/1nb8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nb8 RCSB]</span>
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[[Category: ubp]]
[[Category: ubp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:58 2008''

Revision as of 19:28, 30 March 2008

Image:1nb8.jpg


PDB ID 1nb8

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Gene: USP7 (Homo sapiens)
Activity: Ubiquitin thiolesterase, with EC number 3.1.2.15
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of the catalytic domain of USP7 (HAUSP)


Overview

The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. HAUSP, a representative UBP, specifically deubiquitinates and hence stabilizes the tumor suppressor protein p53. Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. These studies reveal that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm, and Thumb. The leaving ubiquitin moiety is specifically coordinated by the Fingers, with its C terminus placed in the active site between the Palm and the Thumb. Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis.

About this Structure

1NB8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde., Hu M, Li P, Li M, Li W, Yao T, Wu JW, Gu W, Cohen RE, Shi Y, Cell. 2002 Dec 27;111(7):1041-54. PMID:12507430

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