1cmx
From Proteopedia
(New page: 200px<br /><applet load="1cmx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmx, resolution 2.25Å" /> '''STRUCTURAL BASIS FOR...) |
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| - | [[Image:1cmx.gif|left|200px]]<br /><applet load="1cmx" size=" | + | [[Image:1cmx.gif|left|200px]]<br /><applet load="1cmx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cmx, resolution 2.25Å" /> | caption="1cmx, resolution 2.25Å" /> | ||
'''STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES'''<br /> | '''STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The release of ubiquitin from attachment to other proteins and adducts is | + | 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== | ==About this Structure== | ||
| - | 1CMX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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] Full crystallographic information is available from [http:// | + | 1CMX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ubiquitin thiolesterase]] | [[Category: Ubiquitin thiolesterase]] | ||
| - | [[Category: Cohen, R | + | [[Category: Cohen, R E.]] |
| - | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
| - | [[Category: Johnston, S | + | [[Category: Johnston, S C.]] |
| - | [[Category: Riddle, S | + | [[Category: Riddle, S M.]] |
[[Category: cysteine protease]] | [[Category: cysteine protease]] | ||
[[Category: deubiquitinating enzyme]] | [[Category: deubiquitinating enzyme]] | ||
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[[Category: ubiquitin hydrolase]] | [[Category: ubiquitin hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:39 2008'' |
Revision as of 10:07, 21 February 2008
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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]. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 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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