1uch: Difference between revisions
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'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION''' | {{Structure | ||
|PDB= 1uch |SIZE=350|CAPTION= <scene name='initialview01'>1uch</scene>, resolution 1.80Å | |||
|SITE= <scene name='pdbsite=CAT:Active+Site+Residues'>CAT</scene> | |||
|LIGAND= | |||
|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] | |||
|GENE= | |||
}} | |||
'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1UCH is a [ | 1UCH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9233788 9233788] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin conjugation]] | [[Category: ubiquitin conjugation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:30:11 2008'' | ||
Revision as of 12:30, 20 March 2008
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| 1uch, resolution 1.80Å | |||||||||||||
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| Sites: | CAT | ||||||||||||
| Activity: | Ubiquitin thiolesterase, with EC number 3.1.2.15 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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