1tg6

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{{Seed}}
 
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[[Image:1tg6.png|left|200px]]
 
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==Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP==
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The line below this paragraph, containing "STRUCTURE_1tg6", creates the "Structure Box" on the page.
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<StructureSection load='1tg6' size='340' side='right'caption='[[1tg6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1tg6]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TG6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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 id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_1tg6| PDB=1tg6 | SCENE= }}
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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=1tg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg6 OCA], [https://pdbe.org/1tg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tg6 RCSB], [https://www.ebi.ac.uk/pdbsum/1tg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tg6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPP_HUMAN CLPP_HUMAN] Clp cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tg/1tg6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1tg6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have determined a 2.1 A crystal structure for human mitochondrial ClpP (hClpP), the proteolytic component of the ATP-dependent ClpXP protease. HClpP has a structure similar to that of the bacterial enzyme, with the proteolytic active sites sequestered within an aqueous chamber formed by face-to-face assembly of the two heptameric rings. The hydrophobic N-terminal peptides of the subunits are bound within the narrow (12 A) axial channel, positioned to interact with unfolded substrates translocated there by the associated ClpX chaperone. Mutation or deletion of these residues causes a drastic decrease in ClpX-mediated protein and peptide degradation. Residues 8-16 form a mobile loop that extends above the ring surface and is also required for activity. The 28 amino acid C-terminal domain, a unique feature of mammalian ClpP proteins, lies on the periphery of the ring, with its proximal portion forming a loop that extends out from the ring surface. Residues at the start of the C-terminal domain impinge on subunit interfaces within the ring and affect heptamer assembly and stability. We propose that the N-terminal peptide of ClpP is a structural component of the substrate translocation channel and may play an important functional role as well.
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===Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP===
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Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.,Kang SG, Maurizi MR, Thompson M, Mueser T, Ahvazi B J Struct Biol. 2004 Dec;148(3):338-52. PMID:15522782<ref>PMID:15522782</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tg6" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15522782}}, adds the Publication Abstract to the page
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*[[Clp protease 3D structures|Clp protease 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15522782 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15522782}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1TG6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TG6 OCA].
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==Reference==
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Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP., Kang SG, Maurizi MR, Thompson M, Mueser T, Ahvazi B, J Struct Biol. 2004 Dec;148(3):338-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15522782 15522782]
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[[Category: Endopeptidase Clp]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ahvazi, B.]]
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[[Category: Ahvazi B]]
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[[Category: Kang, S G.]]
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[[Category: Kang SG]]
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[[Category: Maurizi, M R.]]
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[[Category: Maurizi MR]]
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[[Category: Mueser, T.]]
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[[Category: Mueser T]]
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[[Category: Thompson, M.]]
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[[Category: Thompson M]]
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[[Category: Atp-dependent protease]]
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[[Category: Clp/hsp 100]]
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[[Category: Mitochondrial clpp]]
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[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:35:53 2008''
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Current revision

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP

PDB ID 1tg6

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