1uch

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[[Image:1uch.jpg|left|200px]]
[[Image:1uch.jpg|left|200px]]
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{{Structure
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|PDB= 1uch |SIZE=350|CAPTION= <scene name='initialview01'>1uch</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1uch", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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>
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{{STRUCTURE_1uch| PDB=1uch | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uch OCA], [http://www.ebi.ac.uk/pdbsum/1uch PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uch RCSB]</span>
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'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION'''
'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION'''
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[[Category: Larsen, C N.]]
[[Category: Larsen, C N.]]
[[Category: Wilkinson, K D.]]
[[Category: Wilkinson, K D.]]
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[[Category: c-terminal hydrolase]]
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[[Category: C-terminal hydrolase]]
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[[Category: cysteine protease]]
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[[Category: Cysteine protease]]
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[[Category: deubiquitinating enzyme]]
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[[Category: Deubiquitinating enzyme]]
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[[Category: ubiquitin]]
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[[Category: Ubiquitin]]
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[[Category: ubiquitin conjugation]]
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[[Category: Ubiquitin conjugation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:02:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:27 2008''
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Revision as of 08:02, 3 May 2008

Image:1uch.jpg

Template:STRUCTURE 1uch

DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION


Overview

Ubiquitin C-terminal hydrolases catalyze the removal of adducts from the C-terminus of ubiquitin. We have determined the crystal structure of the recombinant human Ubiquitin C-terminal Hydrolase (UCH-L3) by X-ray crystallography at 1.8 A resolution. The structure is comprised of a central antiparallel beta-sheet flanked on both sides by alpha-helices. The beta-sheet and one of the helices resemble the well-known papain-like cysteine proteases, with the greatest similarity to cathepsin B. This similarity includes the UCH-L3 active site catalytic triad of Cys95, His169 and Asp184, and the oxyanion hole residue Gln89. Papain and UCH-L3 differ, however, in strand and helix connectivity, which in the UCH-L3 structure includes a disordered 20 residue loop (residues 147-166) that is positioned over the active site and may function in the definition of substrate specificity. Based upon analogy with inhibitor complexes of the papain-like enzymes, we propose a model describing the binding of ubiquitin to UCH-L3. The UCH-L3 active site cleft appears to be masked in the unliganded structure by two different segments of the enzyme (residues 9-12 and 90-94), thus implying a conformational change upon substrate binding and suggesting a mechanism to limit non-specific hydrolysis.

About this Structure

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

Reference

Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution., Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP, EMBO J. 1997 Jul 1;16(13):3787-96. PMID:9233788 Page seeded by OCA on Sat May 3 11:02:17 2008

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