1uch
From Proteopedia
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| - | [[Image:1uch.jpg|left|200px]]<br /><applet load="1uch" size=" | + | [[Image:1uch.jpg|left|200px]]<br /><applet load="1uch" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uch, resolution 1.80Å" /> | caption="1uch, resolution 1.80Å" /> | ||
'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION'''<br /> | '''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Known structural/functional Site: <scene name='pdbsite=CAT:Active Site Residues'>CAT</scene>. Full crystallographic information is available from [http:// | + | 1UCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Known structural/functional Site: <scene name='pdbsite=CAT:Active+Site+Residues'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ubiquitin conjugation]] | [[Category: ubiquitin conjugation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:02:47 2008'' |
Revision as of 08:02, 3 February 2008
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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. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 Known structural/functional Site: . 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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