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Ubiquitin
From Proteopedia
(New page: NMR Structure of Ubiquitin, 1d3z {{STRUCTURE_1d3z| PDB=1d3z | SIZE=300| SCENE= |right|CAPTION=Ubiquitin, 1d3z }} Ubiquitin (UBB) is found...) |
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[[Image:1d3z.png|left|200px|thumb|NMR Structure of Ubiquitin, [[1d3z]]]] | [[Image:1d3z.png|left|200px|thumb|NMR Structure of Ubiquitin, [[1d3z]]]] | ||
| - | {{STRUCTURE_1d3z| PDB=1d3z | SIZE=300| SCENE= |right|CAPTION=Ubiquitin, [[1d3z]] }} | + | {{STRUCTURE_1d3z| PDB=1d3z | SIZE=300| SCENE=Ubiquitin/Cv/1 |right|CAPTION=Ubiquitin, [[1d3z]] }} |
| - | [[Ubiquitin]] (UBB) is found in almost all cells. It binds to proteins tagging them for destruction in the proteasome. UBB is activated by the UBB-activating enzymes E1, E2 and E3. UBB+1 is a frameshifted mutant of UBB observed in several diseases. A dimer of UBB (DiUBB) is formed by linkage of K48 to the C-terminus of a second UBB molecule. At least 4 UBB molecules are needed to tag a protein for the proteasome. | + | [[Ubiquitin]] (UBB) is found in almost all cells. It binds to proteins tagging them for destruction in the proteasome. UBB is activated by the UBB-activating enzymes E1, E2 and E3. UBB+1 is a frameshifted mutant of UBB observed in several diseases. A dimer of UBB (DiUBB) is formed by linkage of K48 to the C-terminus of a second UBB molecule. At least 4 UBB molecules are needed to tag a protein for the proteasome. The images at the left and at the right correspond to one representative Ubiquitin, ''i.e.'' the NMR structure of human Ubiquitin ([[1d3z]]). |
| + | {{TOC limit|limit=2}} | ||
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| + | == 3D Structures of Ubiquitin == | ||
| + | |||
| + | |||
| + | |||
| + | |||
| + | === Ubiquitin === | ||
| - | Ubiquitin | ||
2kn5, 2klg, 2jzz, 2pe9, 2pea, 1g6j, 1d3z – hUBB – NMR | 2kn5, 2klg, 2jzz, 2pe9, 2pea, 1g6j, 1d3z – hUBB – NMR | ||
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2zcc – bUBB - bovine | 2zcc – bUBB - bovine | ||
| - | Ubiquitin+UBB-activating enzymes | + | |
| + | === Ubiquitin+UBB-activating enzymes === | ||
| + | |||
3cmm – yUBB+E1 | 3cmm – yUBB+E1 | ||
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3jvz, 3jw0 – hUBB+E2+E3 | 3jvz, 3jw0 – hUBB+E2+E3 | ||
| - | Ubiquitin+1 mutant | + | |
| + | === Ubiquitin+1 mutant === | ||
| + | |||
2kx0 – hUBB+1 – human – NMR | 2kx0 – hUBB+1 – human – NMR | ||
3k9o – hUBB+1+E2 | 3k9o – hUBB+1+E2 | ||
| - | Ubiquitin dimer | + | |
| + | === Ubiquitin dimer === | ||
| + | |||
2xk5, 3nob, 2xew, 3h7p, 3h7s, 2w9n, 2jf5 – hDiUBB | 2xk5, 3nob, 2xew, 3h7p, 3h7s, 2w9n, 2jf5 – hDiUBB | ||
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2bgf – hDiUBB – chemical relaxation | 2bgf – hDiUBB – chemical relaxation | ||
| - | Ubiquitin tetramer | + | |
| + | === Ubiquitin tetramer === | ||
| + | |||
3alb, 3hm3, 2o6v, 1f9j, 1tbe – tetra-hUBB | 3alb, 3hm3, 2o6v, 1f9j, 1tbe – tetra-hUBB | ||
| - | Ubiquitin bound to protein | + | |
| + | === Ubiquitin bound to protein === | ||
| + | |||
3ofi – hUBB+insulin protease | 3ofi – hUBB+insulin protease | ||
3n3k, 3ifw, 3kvf, 3kw5, 3irt, 3mtn, 3ihp – hUBB (mutant)+hUBB carboxyl-terminal esterase catalytic domain | 3n3k, 3ifw, 3kvf, 3kw5, 3irt, 3mtn, 3ihp – hUBB (mutant)+hUBB carboxyl-terminal esterase catalytic domain | ||
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1otr – yUBB+CUE2 | 1otr – yUBB+CUE2 | ||
| - | Ubiquitin dimer bound to protein | + | |
| + | === Ubiquitin dimer bound to protein === | ||
| + | |||
3a9j, 3a9k, 2wwz, 2wx0, 2wx1 – hDiUBB+mitogen-activated protein kinase | 3a9j, 3a9k, 2wwz, 2wx0, 2wx1 – hDiUBB+mitogen-activated protein kinase | ||
| - | 3jsv, 2zvn, 2zvo – hDiUBB+NF- | + | 3jsv, 2zvn, 2zvo – hDiUBB+NF-κ-b essential modulator |
2kde, 2kdf – DiUBB+26S proteasome non-ATPase regulatory subunit – NMR | 2kde, 2kdf – DiUBB+26S proteasome non-ATPase regulatory subunit – NMR | ||
3a1q – mDiUBB+UBB interaction motif-containing protein – mouse | 3a1q – mDiUBB+UBB interaction motif-containing protein – mouse | ||
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2znv – mDiUBB+hAMSH-like protease | 2znv – mDiUBB+hAMSH-like protease | ||
| - | Ubiquitin + ions | + | |
| + | === Ubiquitin + ions === | ||
3h1u – bUBB+Cd | 3h1u – bUBB+Cd | ||
3ehv, 3eec, 3efu – hUBB+ions | 3ehv, 3eec, 3efu – hUBB+ions | ||
Revision as of 14:17, 20 September 2010
Ubiquitin (UBB) is found in almost all cells. It binds to proteins tagging them for destruction in the proteasome. UBB is activated by the UBB-activating enzymes E1, E2 and E3. UBB+1 is a frameshifted mutant of UBB observed in several diseases. A dimer of UBB (DiUBB) is formed by linkage of K48 to the C-terminus of a second UBB molecule. At least 4 UBB molecules are needed to tag a protein for the proteasome. The images at the left and at the right correspond to one representative Ubiquitin, i.e. the NMR structure of human Ubiquitin (1d3z).
Contents |
3D Structures of Ubiquitin
Ubiquitin
2kn5, 2klg, 2jzz, 2pe9, 2pea, 1g6j, 1d3z – hUBB – NMR 2ojr, 2nr2, 2fcq, 1ubi, 1ubq - hUBB 2zcb, 2gbj, 2gbk, 2gbm, 2gbn, 2gbr, 2fcm, 2fcn, 2fcs, 1yiw, 1yj1, 1sif, 1ogw - hUBB (mutant) 1c3t, 1ud7 - hUBB (mutant) - NMR 1gjz – hUBB N-terminal – NMR 1e0q - hUBB N-terminal (mutant) – NMR 2k39 – UBB – Xenopus laevis – NMR 2jwz, 1zw7 – yUBB (mutant) – yeast 1cmx – yUBB (modified) 2zcc – bUBB - bovine
Ubiquitin+UBB-activating enzymes
3cmm – yUBB+E1 3k9p, 3a33 – hUBB+E2 2gmi - hUBB+E2+MMS2 2kjh, 1zgu – hUBB (mutant)+E2 3jvz, 3jw0 – hUBB+E2+E3
Ubiquitin+1 mutant
2kx0 – hUBB+1 – human – NMR 3k9o – hUBB+1+E2
Ubiquitin dimer
2xk5, 3nob, 2xew, 3h7p, 3h7s, 2w9n, 2jf5 – hDiUBB 3m3j, 1aar – bDiUBB 2bgf – hDiUBB – chemical relaxation
Ubiquitin tetramer
3alb, 3hm3, 2o6v, 1f9j, 1tbe – tetra-hUBB
Ubiquitin bound to protein
3ofi – hUBB+insulin protease 3n3k, 3ifw, 3kvf, 3kw5, 3irt, 3mtn, 3ihp – hUBB (mutant)+hUBB carboxyl-terminal esterase catalytic domain 3i3t, 2ibi, 2ayo, 1nbf - hUBB+hUBB carboxyl-terminal hydrolase catalytic domain 2hd5 - bUBB+hUBB carboxyl-terminal hydrolase catalytic domain 3ldz – bUBB+signal transducing adapter molecule 2khw – hUBB+immunoglobulin G-binding protein G 2kdi – yUBB/UIM fusion 1v80, 1v81 – bUBB/L40 ribosomal protein fusion - NMR 1yx5, 1yx6 - hUBB+26S proteasome non-ATPase regulatory subunit – NMR 2k6d – hUBB+SH3 domain-containing kinase-binding protein – NMR 2z59 – hUBB+mProtein Adhesion-regulating molecule 1 2jy6 – hUBB+hUbiquilin – NMR 3by4, 3c0r – hUBB+yUBB thioesterase 2jt4 – yUBB fragment+cytoskeleton assembly control protein 2hth – hUBB+vacuolar protein sorting protein 2dx5, 1p3q - bUBB+vacuolar protein sorting protein 1q0w - yUBB+vacuolar protein sorting protein 2g3q – yUBB+EDE1 UBA 2c7m, 2c7n, 2fid, 2fif – bUBB+RAB guanine nucleotide exchange factor 2d3g – bUBB+HRS-UIM 1wrd – bUBB+TOM1 GAT domain 1wr6, 1yd8 - bUBB+GGA3 GAT domain 1wr1 – yUBB+DSK2P UBA 1s1q – hUBB+tumor susceptibility gene 101 protein 1q5w – hUBB+NPL4 zinc-fingers 1uzx – bUBB+VPS23 UEV 1otr – yUBB+CUE2
Ubiquitin dimer bound to protein
3a9j, 3a9k, 2wwz, 2wx0, 2wx1 – hDiUBB+mitogen-activated protein kinase 3jsv, 2zvn, 2zvo – hDiUBB+NF-κ-b essential modulator 2kde, 2kdf – DiUBB+26S proteasome non-ATPase regulatory subunit – NMR 3a1q – mDiUBB+UBB interaction motif-containing protein – mouse 3dvg, 3dvn – hDiUBB+IGG1 fab light&heavy chains 2znv – mDiUBB+hAMSH-like protease
Ubiquitin + ions
3h1u – bUBB+Cd 3ehv, 3eec, 3efu – hUBB+ions
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, David Canner, Jaime Prilusky
