2ayo: Difference between revisions
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[[Image:2ayo.gif|left|200px]] | [[Image:2ayo.gif|left|200px]] | ||
'''Structure of USP14 bound to ubquitin aldehyde''' | {{Structure | ||
|PDB= 2ayo |SIZE=350|CAPTION= <scene name='initialview01'>2ayo</scene>, resolution 3.5Å | |||
|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= USP14, TGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Structure of USP14 bound to ubquitin aldehyde''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2AYO is a [ | 2AYO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYO OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16211010 16211010] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: usp14]] | [[Category: usp14]] | ||
''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 15:55:27 2008'' | ||
Revision as of 16:55, 20 March 2008
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| , resolution 3.5Å | |||||||
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| Gene: | USP14, TGT (Homo sapiens) | ||||||
| Activity: | Ubiquitin thiolesterase, with EC number 3.1.2.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of USP14 bound to ubquitin aldehyde
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
About this StructureAbout this Structure
2AYO is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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