2ayn

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(New page: 200px<br /> <applet load="2ayn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ayn, resolution 3.2&Aring;" /> '''Structure of USP14, ...)
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<applet load="2ayn" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2ayn, resolution 3.2&Aring;" />
caption="2ayn, resolution 3.2&Aring;" />
'''Structure of USP14, a proteasome-associated deubiquitinating enzyme'''<br />
'''Structure of USP14, a proteasome-associated deubiquitinating enzyme'''<br />
==Overview==
==Overview==
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The ubiquitin-specific processing protease (UBP) family of, deubiquitinating enzymes plays an essential role in numerous cellular, processes. Mammalian USP14 (Ubp6 in yeast) is unique among known UBP, enzymes in that it is activated catalytically upon specific association, with the 26S proteasome. Here, we report the crystal structures of the, 45-kDa catalytic domain of USP14 in isolation and in a complex with, ubiquitin aldehyde, which reveal distinct structural features. In the, absence of ubiquitin binding, the catalytic cleft leading to the active, site of USP14 is blocked by two surface loops. Binding by ubiquitin, induces a significant conformational change that translocates the two, surface loops thereby allowing access of the ubiquitin C-terminus to the, active site. These structural observations, in conjunction with, biochemical characterization, identify important regulatory mechanisms for, USP14.
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The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. Mammalian USP14 (Ubp6 in yeast) is unique among known UBP enzymes in that it is activated catalytically upon specific association with the 26S proteasome. Here, we report the crystal structures of the 45-kDa catalytic domain of USP14 in isolation and in a complex with ubiquitin aldehyde, which reveal distinct structural features. In the absence of ubiquitin binding, the catalytic cleft leading to the active site of USP14 is blocked by two surface loops. Binding by ubiquitin induces a significant conformational change that translocates the two surface loops thereby allowing access of the ubiquitin C-terminus to the active site. These structural observations, in conjunction with biochemical characterization, identify important regulatory mechanisms for USP14.
==About this Structure==
==About this Structure==
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2AYN 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AYN OCA].
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2AYN 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYN OCA].
==Reference==
==Reference==
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[[Category: Ubiquitin thiolesterase]]
[[Category: Ubiquitin thiolesterase]]
[[Category: Hu, M.]]
[[Category: Hu, M.]]
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[[Category: Jeffrey, P.D.]]
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[[Category: Jeffrey, P D.]]
[[Category: Li, P.]]
[[Category: Li, P.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: usp14]]
[[Category: usp14]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:56:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:25 2008''

Revision as of 14:32, 21 February 2008


2ayn, resolution 3.2Å

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Structure of USP14, a proteasome-associated deubiquitinating enzyme

Overview

The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. Mammalian USP14 (Ubp6 in yeast) is unique among known UBP enzymes in that it is activated catalytically upon specific association with the 26S proteasome. Here, we report the crystal structures of the 45-kDa catalytic domain of USP14 in isolation and in a complex with ubiquitin aldehyde, which reveal distinct structural features. In the absence of ubiquitin binding, the catalytic cleft leading to the active site of USP14 is blocked by two surface loops. Binding by ubiquitin induces a significant conformational change that translocates the two surface loops thereby allowing access of the ubiquitin C-terminus to the active site. These structural observations, in conjunction with biochemical characterization, identify important regulatory mechanisms for USP14.

About this Structure

2AYN is a Single protein structure of sequence from Homo sapiens. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 Full crystallographic information is available from OCA.

Reference

Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14., Hu M, Li P, Song L, Jeffrey PD, Chenova TA, Wilkinson KD, Cohen RE, Shi Y, EMBO J. 2005 Nov 2;24(21):3747-56. Epub 2005 Oct 6. PMID:16211010

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