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| | ==Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4, P61A Mutant== | | ==Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4, P61A Mutant== |
| - | <StructureSection load='2wg6' size='340' side='right' caption='[[2wg6]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='2wg6' size='340' side='right'caption='[[2wg6]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wg6]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WG6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wg6]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WG6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rb5|1rb5]], [[1unt|1unt]], [[1gcm|1gcm]], [[1llm|1llm]], [[2zta|2zta]], [[1unw|1unw]], [[1uo2|1uo2]], [[1ce9|1ce9]], [[2ccf|2ccf]], [[1tmz|1tmz]], [[1zil|1zil]], [[2ccn|2ccn]], [[1w5l|1w5l]], [[1rb6|1rb6]], [[1unz|1unz]], [[1zij|1zij]], [[1w5k|1w5k]], [[1piq|1piq]], [[1unx|1unx]], [[1uny|1uny]], [[1zik|1zik]], [[1ysa|1ysa]], [[1w5h|1w5h]], [[1ij2|1ij2]], [[1unv|1unv]], [[1uo3|1uo3]], [[1ij0|1ij0]], [[2cce|2cce]], [[1unu|1unu]], [[1w5g|1w5g]], [[1ld4|1ld4]], [[2b22|2b22]], [[2b1f|2b1f]], [[1uo0|1uo0]], [[1uo1|1uo1]], [[1swi|1swi]], [[1w5i|1w5i]], [[2dgc|2dgc]], [[2d3e|2d3e]], [[1nkn|1nkn]], [[1kql|1kql]], [[1gcl|1gcl]], [[1zii|1zii]], [[1rb4|1rb4]], [[1uo5|1uo5]], [[1ihq|1ihq]], [[1ij3|1ij3]], [[1zta|1zta]], [[1uo4|1uo4]], [[1w5j|1w5j]], [[1ij1|1ij1]], [[1dgc|1dgc]], [[1rb1|1rb1]], [[1zim|1zim]], [[1gzl|1gzl]], [[2bni|2bni]], [[2wg5|2wg5]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_ATPase Proteasome ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.8 3.6.4.8] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wg6 OCA], [https://pdbe.org/2wg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wg6 RCSB], [https://www.ebi.ac.uk/pdbsum/2wg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wg6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wg6 OCA], [http://pdbe.org/2wg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wg6 RCSB], [http://www.ebi.ac.uk/pdbsum/2wg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wg6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST]] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. | + | [https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.[https://www.uniprot.org/uniprot/PAN_ARCFU PAN_ARCFU] ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (Probable).<ref>PMID:19481487</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Gcn4|Gcn4]] | + | *[[Gcn4 3D Structures|Gcn4 3D Structures]] |
| | + | *[[Gnc4 3D Structures|Gnc4 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arcfu]] | + | [[Category: Archaeoglobus fulgidus]] |
| - | [[Category: Proteasome ATPase]] | + | [[Category: Large Structures]] |
| - | [[Category: Djuranovic, S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hartmann, M D]] | + | [[Category: Djuranovic S]] |
| - | [[Category: Lupas, A N]] | + | [[Category: Hartmann MD]] |
| - | [[Category: Ursinus, A]] | + | [[Category: Lupas AN]] |
| - | [[Category: Zeth, K]] | + | [[Category: Ursinus A]] |
| - | [[Category: Aaa protein]]
| + | [[Category: Zeth K]] |
| - | [[Category: Activator]]
| + | |
| - | [[Category: Atp-binding amino-acid biosynthesis]]
| + | |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Chaperone activity]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Ob fold]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Proteasome]]
| + | |
| - | [[Category: Substrate recognition]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription hydrolase complex]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
GCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.PAN_ARCFU ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (Probable).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (N domains) are thought to mediate substrate recognition. The N domains of an archaeal proteasomal ATPase, Archaeoglobus fulgidus PAN, and of its actinobacterial homolog, Rhodococcus erythropolis ARC, form hexameric rings, whose subunits consist of an N-terminal coiled coil and a C-terminal OB domain. In ARC-N, the OB domains are duplicated and form separate rings. PAN-N and ARC-N can act as chaperones, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras, even when these include coiled coils and OB domains from unrelated proteins. The structures suggest a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the OB rings.
Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases.,Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K. Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487 doi:10.1016/j.molcel.2009.04.030
- ↑ Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K. Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487 doi:10.1016/j.molcel.2009.04.030
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