This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Thioesterase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 25: Line 25:
[[1q4t]] - ArTE + 4-hydroxyphenyl CoA<br />
[[1q4t]] - ArTE + 4-hydroxyphenyl CoA<br />
[[1q4u]] - ArTE + 4-hydroxybenzyl CoA<br />
[[1q4u]] - ArTE + 4-hydroxybenzyl CoA<br />
-
[[3r32]], [[3r35]], [[3r37]], [[3r38]], [[3r3c]], [[3r3d]], [[3r3f]], [[3tea]] - ArTE (mutant) + 4-hydroxyphenacyl CoA<br />
+
[[3r32]], [[3r35]], [[3r37]], [[3r38]], [[3r3b]], [[3r3c]], [[3r3d]], [[3r3f]], [[3tea]] - ArTE (mutant) + 4-hydroxyphenacyl CoA<br />
-
[[3r3a]] - ArTE (mutant) + 4-hydroxybenzoate<br />
+
[[3r36]] - ArTE (mutant) + 4-hydroxybenzoate<br />
 +
[[3r3a]] - ArTE (mutant) + 4-hydroxybenzoate + CoA<br />
[[3r34]] - ArTE (mutant) + CoA<br />
[[3r34]] - ArTE (mutant) + CoA<br />
Line 61: Line 62:
'''Acyl-ACP TE'''
'''Acyl-ACP TE'''
-
[[2ess]] – TE – ''Bacterioides thetaiotaomicron''
+
[[2ess]] – TE – ''Bacterioides thetaiotaomicron''<br />
 +
[[4gak]] – TE – ''Spirosoma linguale''<br />
 +
[[4gwh]] – TE – ''Yersinia pestis''<br />
 +
 
 +
'''ACP-polyene TE'''
 +
 
 +
[[4i4j]] – TE – ''Streptomyces globisporus''<br />
'''Fluoroacetyl-CoA TE'''
'''Fluoroacetyl-CoA TE'''
Line 69: Line 76:
[[3kvu]] – ScTE + acetyl-CoA<br />
[[3kvu]] – ScTE + acetyl-CoA<br />
[[3kvz]], [[3kw1]] – ScTE + FAcOPan<br />
[[3kvz]], [[3kw1]] – ScTE + FAcOPan<br />
-
[[3kx7]], [[3fx8]], [[3p2q]] – ScTE <br />
+
[[3kx7]], [[3kx8]], [[3p2q]] – ScTE <br />
[[3p3f]] – ScTE (mutant) <br />
[[3p3f]] – ScTE (mutant) <br />
[[3p3i]] - ScTE (mutant) + acetate derivative + CoA<br />
[[3p3i]] - ScTE (mutant) + acetate derivative + CoA<br />
 +
 +
'''DHNA-CoA TE'''
 +
 +
[[4k00]] – TE – ''Synechocystis''<br />
 +
[[4k02]] – TE – ''Arabidopsis thaliana''<br />
'''Ubiquitin TE'''
'''Ubiquitin TE'''
Line 167: Line 179:
[[3von]] – hUSP + E2 <BR />
[[3von]] – hUSP + E2 <BR />
[[4ddg]], [[4ddi]] – hUSP + Ub<BR />
[[4ddg]], [[4ddi]] – hUSP + Ub<BR />
-
[[4ddi]] – hUSP (mutant) + Ub<BR />
+
[[4ddi]], [[4i6l]] – hUSP (mutant) + Ub<BR />
[[4dhz]] – hUSP + E2 + Ub<BR />
[[4dhz]] – hUSP + E2 + Ub<BR />
 +
[[4boq]] - hUSP OTU domain <BR />
 +
[[4boz]] - hUSP OTU domain (mutant) + Ub <BR />
 +
[[4bos]] - hUSP OTU domain (mutant) + Ub + OTUD2 peptide<BR />
 +
[[4fjv]] - hUSP OTUB2 + Ub <BR />
[[4dhj]] – nUSP + E2 + Ub - nematode<BR />
[[4dhj]] – nUSP + E2 + Ub - nematode<BR />
[[4dhi]] – nUSP + E2 <BR />
[[4dhi]] – nUSP + E2 <BR />
 +
[[2kzr]] – mUSP UBX-like domain – NMR<br />
 +
[[4kdi]], [[4kdl]] – yUSP UBX-like domain + transitional endoplasmic reticulum ATPase<br />
 +
[[3by4]], [[3c0r]] - yUSP OTU domain + Ub<BR />
[[3znh]] – USP + Ub – Crimean-Congo hemorrhagic fever virus<BR />
[[3znh]] – USP + Ub – Crimean-Congo hemorrhagic fever virus<BR />
Line 178: Line 197:
[[3qmv]], [[3qmw]] – TE –'' Streptomyces coelicolor''
[[3qmv]], [[3qmw]] – TE –'' Streptomyces coelicolor''
 +
'''Orf6 TE'''
 +
 +
[[4i45]] – TE – ''Photobacterium profundum''<br />
-
[[2av9 ]]– TE – ''Pseudomonas aeruginosa''
+
[[2av9]], [[2o5u]], [[2o6b]], [[2o6t]], [[2o6u]], [[3qy3]] – TE – ''Pseudomonas aeruginosa''
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:16, 18 May 2014

Template:STRUCTURE 1u8u

Thioesterase (TE) catalyzes the break of an ester bond to produce acid and alcohol at a thiol group. TEs are substrate-specific. Palmitoyl protein TE removes fatty acids like palmitate from modified cysteine residues during lysosomal degradation. 4-hydroxybenzoyl-CoA TE converts 4-hydroxybenzoyl-CoA to 4-hydroxybenzoate and CoA. Acyl-CoA TE hydrolyzes acyl-CoA to the fatty acid and CoA and is involved in lipid metabolism. Fluoroacetyl-CoA TE from Streptomyces cattleya hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate. Ubiquitin TE (USP) removes conjugated ubiquitin from proteins thus regulating protein level by preventing their degradation.

3D structures of thioesterase

Updated on 18-May-2014

Maristoyl-ACP-specific TE

1tht – TE – Vibrio harveyi

4-hydroxybenzoyl-CoA TE

1bvq – PsTE – Pseudomonas
1lo7 – PsTE + 4-hydroxyphenyl CoA
1lo9 - PsTE (mutant) + 4-hydroxybenzoyl CoA
1lo8 - PsTE + 4-hydroxybenzyl CoA
1q4s - ArTE + 4-hydroxybenzoate – 'Arthrobacter'
1q4t - ArTE + 4-hydroxyphenyl CoA
1q4u - ArTE + 4-hydroxybenzyl CoA
3r32, 3r35, 3r37, 3r38, 3r3b, 3r3c, 3r3d, 3r3f, 3tea - ArTE (mutant) + 4-hydroxyphenacyl CoA
3r36 - ArTE (mutant) + 4-hydroxybenzoate
3r3a - ArTE (mutant) + 4-hydroxybenzoate + CoA
3r34 - ArTE (mutant) + CoA

Palmitoyl protein TE

1eh5 – bTE1 + Palmitate – bovine
1ei9 – bTE1
1exw – bTE1 + hexadecylsulfonyl fluoride
1pja – hTEII – human
3gro - hTEI

Acyl-CoA TE

1c8u – EcTEII – Escherichia coli
1ivn – EcTEI
1jrl – EcTEI (mutant)
1j00 – EcTEI + diethyl phosphono derivative
1v2g, 1u8u - EcTEI + octanoic acid
2v1o – mTE7 hotdog domain – mouse
2q2b – mTE7 C terminal
3hlk – hTE2
3k2i – hTE4
2qq2 - hTE7 C terminal
3fo5 – hTE11 START domain
3b7k – hTE12
3rd7 – TE – Mycobacterium avium
3u0a – TEII – Mycobacterium marinum
1tbu – TE N terminal (peroximal) – yeast

Acyl protein TE

1fj2 – EcTEI

Acyl-ACP TE

2ess – TE – Bacterioides thetaiotaomicron
4gak – TE – Spirosoma linguale
4gwh – TE – Yersinia pestis

ACP-polyene TE

4i4j – TE – Streptomyces globisporus

Fluoroacetyl-CoA TE

3kuv, 3kuw, 3kvi – ScTE (mutant) + acetate derivative – Streptomyces cattleya
3kv7, 3kv8, 3p2r, 3p2s – ScTE + acetate derivative
3kvu – ScTE + acetyl-CoA
3kvz, 3kw1 – ScTE + FAcOPan
3kx7, 3kx8, 3p2q – ScTE
3p3f – ScTE (mutant)
3p3i - ScTE (mutant) + acetate derivative + CoA

DHNA-CoA TE

4k00 – TE – Synechocystis
4k02 – TE – Arabidopsis thaliana

Ubiquitin TE

USP 2

2zfy – hUSP – human
2hd5, 3nhe – hUSP + Ub
1tff – hUSP (mutant)
2ibi – hUSP (mutant) + Ub

USP 3

2qiy – USP + UBP-associated protein – yeast

USP 5

3ihp – hUSP + Ub

USP 7

2ylm, 2f1z – hUSP
2kvr – hUSP UBL domain - NMR
1nb8 – hUSP catalytic domain
1yze – hUSP N terminal domain
2f1w – hUSP TRAF-like domain
2f1x – hUSP TRAF-like domain + p53 peptide
2foj, 2foo – hUSP N terminal domain + p53 peptide
2f1y – hUSP TRAF-like domain + MDM2 peptide
2fop – hUSP N terminal domain + MDM2 peptide
1nbf – hUSP catalytic domain + ubiquitin aldehyde
1yy6 – hUSP N terminal domain + Epstein-Barr nuclear antigen
3mqr, 3mqs – hUSP + peptide
2xxn – hUSP + VIRF-4
4jjq – hUSP (mutant) + E2

USP 8

2a9u – hUSP N terminal domain
2gfo – hUSP catalytic domain
2gwf – hUSP rhodanese domain + ring finger protein
3mhh, 3m99, 4fip, 4fjc, 4fk5 – hUSP + SUS1 + SAGA-associated factors 11, 73
3mhs – hUSP + SUS1 + SAGA-associated factors 11, 73 + Ub
3n3k – hUSP + Ub inhibitor

USP 15

3lmn – hUSP DUSP domain

USP 16

2i50 – hUSP zinc finger domain - NMR

USP 21

3i3t – hUSP + Ub
3mtn – hUSP + Ub inhibitor

USP 28

2lva – hUSP N terminal - NMR

USP 33

2uzg – hUSP zinc finger domain - NMR

USP 37

3ihr – hUSP (mutant)
3a7s – hUSP catalytic domain (mutant)

USP Cyld

2vhf – hUSP

USP L1

3irt – hUSP (mutant)
2len – hUSP (mutant) - NMR
3ifw, 3kvf, 3kw5 – hUSP (mutant) + Ub
4dm9 – hUSP + peptide inhibitor

USP L5

3ris – hUSP catalytic domain
3rii – hUSP catalytic domain (mutant)
3tb3 – hUSP UCH domain (mutant)

USP ZranB1

3zrh – hUSP

USP OTUB1

3von – hUSP + E2
4ddg, 4ddi – hUSP + Ub
4ddi, 4i6l – hUSP (mutant) + Ub
4dhz – hUSP + E2 + Ub
4boq - hUSP OTU domain
4boz - hUSP OTU domain (mutant) + Ub
4bos - hUSP OTU domain (mutant) + Ub + OTUD2 peptide
4fjv - hUSP OTUB2 + Ub
4dhj – nUSP + E2 + Ub - nematode
4dhi – nUSP + E2
2kzr – mUSP UBX-like domain – NMR
4kdi, 4kdl – yUSP UBX-like domain + transitional endoplasmic reticulum ATPase
3by4, 3c0r - yUSP OTU domain + Ub

3znh – USP + Ub – Crimean-Congo hemorrhagic fever virus

RedJ TE

3qmv, 3qmw – TE – Streptomyces coelicolor

Orf6 TE

4i45 – TE – Photobacterium profundum

2av9, 2o5u, 2o6b, 2o6t, 2o6u, 3qy3 – TE – Pseudomonas aeruginosa

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools