2wg5

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==PROTEASOME-ACTIVATING NUCLEOTIDASE (PAN) N-DOMAIN (57-134) FROM ARCHAEOGLOBUS FULGIDUS FUSED TO GCN4==
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<StructureSection load='2wg5' size='340' side='right' caption='[[2wg5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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==Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4==
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<StructureSection load='2wg5' size='340' side='right'caption='[[2wg5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2wg5]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WG5 OCA]. <br>
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<table><tr><td colspan='2'>[[2wg5]] 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=2WG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WG5 FirstGlance]. <br>
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</td></tr><tr><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]], [[2bni|2bni]], [[1gzl|1gzl]], [[2wg6|2wg6]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wg5 OCA], [https://pdbe.org/2wg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wg5 RCSB], [https://www.ebi.ac.uk/pdbsum/2wg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wg5 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wg5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wg5 RCSB], [http://www.ebi.ac.uk/pdbsum/2wg5 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wg/2wg5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wg/2wg5_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wg5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
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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<ref>PMID:19481487</ref>
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<ref>PMID:19481487</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2wg5" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
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*[[Gnc4 3D Structures|Gnc4 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Proteasome ATPase]]
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[[Category: Archaeoglobus fulgidus]]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Djuranovic, S.]]
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[[Category: Djuranovic S]]
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[[Category: Hartmann, M D.]]
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[[Category: Hartmann MD]]
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[[Category: Lupas, A N.]]
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[[Category: Lupas AN]]
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[[Category: Ursinus, A.]]
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[[Category: Ursinus A]]
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[[Category: Zeth, K.]]
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[[Category: Zeth K]]
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[[Category: Aaa protein]]
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[[Category: Activator]]
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[[Category: Atp-binding amino-acid biosynthesis]]
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[[Category: Atpase]]
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[[Category: Chaperone activity]]
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[[Category: Dna-binding]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Ob fold]]
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[[Category: Phosphoprotein]]
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[[Category: Proteasome]]
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[[Category: Substrate recognition]]
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[[Category: Transcription]]
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[[Category: Transcription hydrolase complex]]
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[[Category: Transcription regulation]]
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Current revision

Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4

PDB ID 2wg5

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