1um8

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{{Seed}}
 
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[[Image:1um8.png|left|200px]]
 
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==Crystal structure of helicobacter pylori ClpX==
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The line below this paragraph, containing "STRUCTURE_1um8", creates the "Structure Box" on the page.
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<StructureSection load='1um8' size='340' side='right'caption='[[1um8]], [[Resolution|resolution]] 2.60&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'>[[1um8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UM8 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]] 2.6&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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{{STRUCTURE_1um8| PDB=1um8 | 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=1um8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1um8 OCA], [https://pdbe.org/1um8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1um8 RCSB], [https://www.ebi.ac.uk/pdbsum/1um8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1um8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPX_HELPY CLPX_HELPY] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity).[HAMAP-Rule:MF_00175]
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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/um/1um8_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=1um8 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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ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N-terminal Cys cluster region complexed with ADP, was determined. The overall structure of ClpX is similar to that of heat shock locus U (HslU), consisting of two subdomains, with ADP bound at the subdomain interface. The crystal structure of ClpX reveals that a conserved tripeptide (LGF) is located on the tip of ClpP binding loop extending from the N-terminal subdomain. A hexameric model of ClpX suggests that six tripeptides make hydrophobic contacts with the hydrophobic clefts of the ClpP heptmer asymmetrically. In addition, the nucleotide binding environment provides the structural explanation for the hexameric assembly and the modulation of ATPase activity.
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===Crystal structure of helicobacter pylori ClpX===
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Crystal structure of ClpX molecular chaperone from Helicobacter pylori.,Kim DY, Kim KK J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:14514695<ref>PMID:14514695</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 1um8" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_14514695}}, adds the Publication Abstract to the page
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*[[Clp Protease|Clp Protease]]
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(as it appears on PubMed at http://www.pubmed.gov), where 14514695 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14514695}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1UM8 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UM8 OCA].
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==Reference==
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<ref group="xtra">PMID:14514695</ref><references group="xtra"/>
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[[Category: Helicobacter pylori 26695]]
[[Category: Helicobacter pylori 26695]]
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[[Category: Kim, D Y.]]
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[[Category: Large Structures]]
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[[Category: Kim, K K.]]
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[[Category: Kim DY]]
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[[Category: Clpp binding loop]]
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[[Category: Kim KK]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:54:21 2009''
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Current revision

Crystal structure of helicobacter pylori ClpX

PDB ID 1um8

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