Thioesterase

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Line 52: Line 52:
**[[3r3a]] - ArTE (mutant) + 4-hydroxybenzoate + CoA<br />
**[[3r3a]] - ArTE (mutant) + 4-hydroxybenzoate + CoA<br />
**[[3r34]] - ArTE (mutant) + CoA<br />
**[[3r34]] - ArTE (mutant) + CoA<br />
 +
**[[5lql]] – SaTE – ''Staphylococcus aureus''<br />
*Palmitoyl protein thioesterase
*Palmitoyl protein thioesterase
Line 63: Line 64:
*Acyl-CoA thioesterase
*Acyl-CoA thioesterase
-
**[[1c8u]] – EcTEII – ''Escherichia coli''<br />
+
**[[2pzh]] - TE - ''Helicobacter pylori''<br />
-
**[[1ivn]] – EcTEI<br />
+
**[[3rd7]] – TE – ''Mycobacterium avium''<br />
 +
**[[5t02]] – TE (mutant) + CoA + GDP – ''Neisseria meningitis''<br />
 +
**[[5hz4]], [[5hwf]], [[5egk]] – SaTE (mutant) – ''Staphylococcus aureus''<br />
 +
**[[4egj]] – SaTE + CoA<br />
 +
**[[1ivn]], [[5tic]] – EcTEI – ''Escherichia coli''<br />
**[[1jrl]] – EcTEI (mutant) <br />
**[[1jrl]] – EcTEI (mutant) <br />
**[[1j00]] – EcTEI + diethyl phosphono derivative<br />
**[[1j00]] – EcTEI + diethyl phosphono derivative<br />
**[[1v2g]], [[1u8u]] - EcTEI + octanoic acid<br />
**[[1v2g]], [[1u8u]] - EcTEI + octanoic acid<br />
-
**[[2v1o]] – mTE7 hotdog domain – mouse<br />
+
**[[5tid]], [[5tie]], [[5tif]] - EcTEI (mutant) + octanoic acid<br />
-
**[[2q2b]] – mTE7 C terminal<br />
+
**[[1tbu]] – TEI N terminal (peroximal) – yeast<br />
-
**[[2pzh]] - TE - ''Helicobacter pylori''<br />
+
**[[1c8u]] – EcTEII <br />
 +
**[[3u0a]] – TEII – ''Mycobacterium marinum''<br />
 +
**[[4qfw]] – YpTE II – ''Yersinia pestis''<br />
 +
**[[4r4u]] – YpTE II + CoA<br />
**[[3hlk]] – hTE2<br />
**[[3hlk]] – hTE2<br />
**[[3k2i]] – hTE4<br />
**[[3k2i]] – hTE4<br />
**[[2qq2]] - hTE7 C terminal<br />
**[[2qq2]] - hTE7 C terminal<br />
 +
**[[2v1o]] – mTE7 hotdog domain – mouse<br />
 +
**[[2q2b]] – mTE7 C terminal<br />
**[[3fo5]] – hTE11 START domain<br />
**[[3fo5]] – hTE11 START domain<br />
**[[3b7k]], [[4moc]] – hTE12<br />
**[[3b7k]], [[4moc]] – hTE12<br />
**[[4mob]] – hTE12 + ADP<br />
**[[4mob]] – hTE12 + ADP<br />
-
**[[3rd7]] – TE – ''Mycobacterium avium''<br />
 
-
**[[3u0a]] – TEII – ''Mycobacterium marinum''<br />
 
-
**[[1tbu]] – TE N terminal (peroximal) – yeast<br />
 
-
**[[4qfw]] – YpTE II – ''Yersinia pestis''<br />
 
-
**[[4r4u]] – YpTE II + CoA<br />
 
-
**[[5t02]] – TE (mutant) + CoA + GDP – ''Neisseria meningitis''<br />
 
-
**[[5hz4]], [[5hwf]], [[5egk]] – SaTE (mutant) – ''Staphylococcus aureus''<br />
 
-
**[[4egj]] – SaTE + CoA<br />
 
*Acyl protein thioesterase
*Acyl protein thioesterase
-
**[[1fj2]] – EcTEI
+
**[[1fj2]] – EcTEI<br />
 +
**[[5sym]] – hTE 1 + inhibitor<br />
 +
**[[5syn]] – hTE 2 + inhibitor<br />
*Acyl-ACP thioesterase
*Acyl-ACP thioesterase
Line 137: Line 141:
*Ubiquitin thioesterase 3
*Ubiquitin thioesterase 3
-
**[[2qiy]] – yUSP + USP-associated protein – yeast <BR />
+
**[[2qiy]] – yUSP + USP-associated protein <BR />
*Ubiquitin thioesterase 4
*Ubiquitin thioesterase 4
**[[2y6e]] – hUSP catalytic domain <br />
**[[2y6e]] – hUSP catalytic domain <br />
-
**[[3jyu]] – mUSP N terminal domain - mouse<br />
+
**[[3jyu]] – mUSP N terminal domain <br />
*Ubiquitin thioesterase 5
*Ubiquitin thioesterase 5
Line 192: Line 196:
**[[4zux]] – yUSP + SUS1 + SGF11 +SGF73 + Ub + Histones H3,2, H4, H2A, H2B + DNA<br />
**[[4zux]] – yUSP + SUS1 + SGF11 +SGF73 + Ub + Histones H3,2, H4, H2A, H2B + DNA<br />
**[[3n3k]] – hUSP catalytic domain + Ub<br />
**[[3n3k]] – hUSP catalytic domain + Ub<br />
 +
 +
*Ubiquitin thioesterase 9
 +
 +
**[[5vbd]] – hUSP 9x UBL domain <br />
*Ubiquitin thioesterase 11
*Ubiquitin thioesterase 11
Line 328: Line 336:
**[[4qd8]], [[4dq9]] – PaTE hotdog domain + acyl-CoA derivatives<br />
**[[4qd8]], [[4dq9]] – PaTE hotdog domain + acyl-CoA derivatives<br />
 +
*Thioesterase
 +
 +
**[[5vpj]] – TE – ''Actinomadura verrucosospora''<br />
 +
**[[5dio]], [[5byu]] – TE – ''Legionella pneumophila''<br />
}}
}}

Revision as of 11:27, 7 November 2017

Human ubiquitin esterase 2 (deepskyblue) complex with ubiquitin (green) and zinc+2 ion (grey) (PDB code 2hd5).

Drag the structure with the mouse to rotate

3D structures of thioesterase

Updated on 07-November-2017

5fwi]] – hUSP catalytic + UBL domains 1+2

References

  1. ↑ Cho S, Dawson G. Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras-Akt-caspase pathway in neuroblastoma cells. J Neurochem. 2000 Apr;74(4):1478-88. PMID:10737604
  2. ↑ Zhuang Z, Gartemann KH, Eichenlaub R, Dunaway-Mariano D. Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU. Appl Environ Microbiol. 2003 May;69(5):2707-11. PMID:12732540
  3. ↑ Hunt MC, Alexson SE. The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. PMID:11755680
  4. ↑ Weeks AM, Coyle SM, Jinek M, Doudna JA, Chang MC. Structural and Biochemical Studies of a Fluoroacetyl-CoA-Specific Thioesterase Reveal a Molecular Basis for Fluorine Selectivity. Biochemistry. 2010 Oct 11. PMID:20836570 doi:10.1021/bi101102u
  5. ↑ Jagannathan M, Nguyen T, Gallo D, Luthra N, Brown GW, Saridakis V, Frappier L. A role for USP7 in DNA replication. Mol Cell Biol. 2014 Jan;34(1):132-45. doi: 10.1128/MCB.00639-13. Epub 2013 Nov 4. PMID:24190967 doi:http://dx.doi.org/10.1128/MCB.00639-13
  6. ↑ Jahan AS, Lestra M, Swee LK, Fan Y, Lamers MM, Tafesse FG, Theile CS, Spooner E, Bruzzone R, Ploegh HL, Sanyal S. Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling. Proc Natl Acad Sci U S A. 2016 Feb 9;113(6):E705-14. doi:, 10.1073/pnas.1521763113. Epub 2016 Jan 25. PMID:26811477 doi:http://dx.doi.org/10.1073/pnas.1521763113
  7. ↑ Malhotra S, Morcillo-Suarez C, Nurtdinov R, Rio J, Sarro E, Moreno M, Castillo J, Navarro A, Montalban X, Comabella M. Roles of the ubiquitin peptidase USP18 in multiple sclerosis and the response to interferon-beta treatment. Eur J Neurol. 2013 Oct;20(10):1390-7. doi: 10.1111/ene.12193. Epub 2013 May 22. PMID:23700969 doi:http://dx.doi.org/10.1111/ene.12193
  8. ↑ Huo Y, Khatri N, Hou Q, Gilbert J, Wang G, Man HY. The deubiquitinating enzyme USP46 regulates AMPA receptor ubiquitination and trafficking. J Neurochem. 2015 Sep;134(6):1067-80. doi: 10.1111/jnc.13194. Epub 2015 Jul 16. PMID:26077708 doi:http://dx.doi.org/10.1111/jnc.13194
  9. ↑ Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature. 1995 Aug 17;376(6541):584-7. PMID:7637805 doi:http://dx.doi.org/10.1038/376584a0
  10. ↑ van Diggelen OP, Thobois S, Tilikete C, Zabot MT, Keulemans JL, van Bunderen PA, Taschner PE, Losekoot M, Voznyi YV. Adult neuronal ceroid lipofuscinosis with palmitoyl-protein thioesterase deficiency: first adult-onset patients of a childhood disease. Ann Neurol. 2001 Aug;50(2):269-72. PMID:11506414
  11. ↑ Renatus M, Parrado SG, D'Arcy A, Eidhoff U, Gerhartz B, Hassiepen U, Pierrat B, Riedl R, Vinzenz D, Worpenberg S, Kroemer M. Structural basis of ubiquitin recognition by the deubiquitinating protease USP2. Structure. 2006 Aug;14(8):1293-302. PMID:16905103 doi:10.1016/j.str.2006.06.012

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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