1cmx
From Proteopedia
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| - | [[Image:1cmx.gif|left|200px]] | + | [[Image:1cmx.gif|left|200px]] |
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| - | '''STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES''' | + | {{Structure |
| + | |PDB= 1cmx |SIZE=350|CAPTION= <scene name='initialview01'>1cmx</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CMX is a [ | + | 1CMX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMX OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the specificity of ubiquitin C-terminal hydrolases., Johnston SC, Riddle SM, Cohen RE, Hill CP, EMBO J. 1999 Jul 15;18(14):3877-87. PMID:[http:// | + | Structural basis for the specificity of ubiquitin C-terminal hydrolases., Johnston SC, Riddle SM, Cohen RE, Hill CP, EMBO J. 1999 Jul 15;18(14):3877-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10406793 10406793] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ubiquitin thiolesterase]] | [[Category: Ubiquitin thiolesterase]] | ||
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[[Category: ubiquitin hydrolase]] | [[Category: ubiquitin hydrolase]] | ||
| - | ''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 10:26:20 2008'' |
Revision as of 08:26, 20 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Ubiquitin thiolesterase, with EC number 3.1.2.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES
Overview
The release of ubiquitin from attachment to other proteins and adducts is critical for ubiquitin biosynthesis, proteasomal degradation and other cellular processes. De-ubiquitination is accomplished in part by members of the UCH (ubiquitin C-terminal hydrolase) family of enzymes. We have determined the 2.25 A resolution crystal structure of the yeast UCH, Yuh1, in a complex with the inhibitor ubiquitin aldehyde (Ubal). The structure mimics the tetrahedral intermediate in the reaction pathway and explains the very high enzyme specificity. Comparison with a related, unliganded UCH structure indicates that ubiquitin binding is coupled to rearrangements which block the active-site cleft in the absence of authentic substrate. Remarkably, a 21-residue loop that becomes ordered upon binding Ubal lies directly over the active site. Efficiently processed substrates apparently pass through this loop, and constraints on the loop conformation probably function to control UCH specificity.
About this Structure
1CMX is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity of ubiquitin C-terminal hydrolases., Johnston SC, Riddle SM, Cohen RE, Hill CP, EMBO J. 1999 Jul 15;18(14):3877-87. PMID:10406793
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