1xd3

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[[Image:1xd3.gif|left|200px]]
[[Image:1xd3.gif|left|200px]]
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{{Structure
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|PDB= 1xd3 |SIZE=350|CAPTION= <scene name='initialview01'>1xd3</scene>, resolution 1.45&Aring;
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The line below this paragraph, containing "STRUCTURE_1xd3", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GVE:METHYL+4-AMINOBUTANOATE'>GVE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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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/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1xd3| PDB=1xd3 | SCENE= }}
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|RELATEDENTRY=[[1cmx|1CMX]], [[1ubq|1UBQ]], [[1uch|1UCH]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xd3 OCA], [http://www.ebi.ac.uk/pdbsum/1xd3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xd3 RCSB]</span>
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}}
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'''Crystal structure of UCHL3-UbVME complex'''
'''Crystal structure of UCHL3-UbVME complex'''
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[[Category: Ovaa, H.]]
[[Category: Ovaa, H.]]
[[Category: Ploegh, H L.]]
[[Category: Ploegh, H L.]]
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[[Category: active site crossover loop]]
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[[Category: Active site crossover loop]]
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[[Category: enzyme-ligand complex]]
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[[Category: Enzyme-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:52:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:47:56 2008''
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Revision as of 11:52, 3 May 2008

Template:STRUCTURE 1xd3

Crystal structure of UCHL3-UbVME complex


Overview

Ubiquitin C-terminal hydrolases (UCHs) comprise a family of small ubiquitin-specific proteases of uncertain function. Although no cellular substrates have been identified for UCHs, their highly tissue-specific expression patterns and the association of UCH-L1 mutations with human disease strongly suggest a critical role. The structure of the yeast UCH Yuh1-ubiquitin aldehyde complex identified an active site crossover loop predicted to limit the size of suitable substrates. We report the 1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethylester, an inhibitor that forms a covalent adduct with the active site cysteine of ubiquitin-specific proteases. This structure confirms the predicted mechanism of the inhibitor and allows the direct comparison of a UCH family enzyme in the free and ligand-bound state. We also show the efficient hydrolysis by human UCH-L3 of a 13-residue peptide in isopeptide linkage with ubiquitin, consistent with considerable flexibility in UCH substrate size. We propose a model for the catalytic cycle of UCH family members which accounts for the hydrolysis of larger ubiquitin conjugates.

About this Structure

1XD3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate., Misaghi S, Galardy PJ, Meester WJ, Ovaa H, Ploegh HL, Gaudet R, J Biol Chem. 2005 Jan 14;280(2):1512-20. Epub 2004 Nov 5. PMID:15531586 Page seeded by OCA on Sat May 3 14:52:37 2008

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