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1kp8

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(New page: 200px<br /><applet load="1kp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kp8, resolution 2.00&Aring;" /> '''Structural Basis for...)
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[[Image:1kp8.gif|left|200px]]<br /><applet load="1kp8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kp8, resolution 2.00&Aring;" />
 
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'''Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution'''<br />
 
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==Overview==
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==Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution==
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Nucleotide regulates the affinity of the bacterial chaperonin GroEL for, protein substrates. GroEL binds protein substrates with high affinity in, the absence of ATP and with low affinity in its presence. We report the, crystal structure of (GroEL-KMgATP)(14) refined to 2.0 A resolution in, which the ATP triphosphate moiety is directly coordinated by both K(+) and, Mg(2+). Upon the binding of KMgATP, we observe previously unnoticed domain, rotations and a 102 degrees rotation of the apical domain surface helix I., Two major consequences are a large lateral displacement of, and a dramatic, reduction of hydrophobicity in, the apical domain surface. These results, provide a basis for the nucleotide-dependent regulation of protein, substrate binding and suggest a mechanism for GroEL-assisted protein, folding by forced unfolding.
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<StructureSection load='1kp8' size='340' side='right'caption='[[1kp8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kp8]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1der 1der]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KP8 FirstGlance]. <br>
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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&#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=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1kp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kp8 OCA], [https://pdbe.org/1kp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kp8 RCSB], [https://www.ebi.ac.uk/pdbsum/1kp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kp8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
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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/kp/1kp8_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=1kp8 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1KP8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with K, SO4, MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1DER. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KP8 OCA].
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution., Wang J, Boisvert DC, J Mol Biol. 2003 Apr 4;327(4):843-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12654267 12654267]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Wang, J.]]
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[[Category: Wang J]]
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[[Category: ATP]]
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[[Category: K]]
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[[Category: MG]]
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[[Category: SO4]]
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[[Category: assisted protein folding]]
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[[Category: chaperonin]]
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[[Category: groel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:33:36 2007''
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Current revision

Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution

PDB ID 1kp8

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