1xew

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(New page: 200px<br /><applet load="1xew" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xew, resolution 2.0&Aring;" /> '''Structural biochemist...)
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[[Image:1xew.gif|left|200px]]<br /><applet load="1xew" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xew, resolution 2.0&Aring;" />
 
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'''Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.'''<br />
 
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==Overview==
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==Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.==
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Structural maintenance of chromosome (SMC) proteins play a central role in, higher-order chromosome structure in all kingdoms of life. SMC proteins, consist of a long coiled-coil domain that joins an ATP binding cassette, (ABC) ATPase domain on one side and a dimerization domain on the other, side. SMC proteins require ATP binding or hydrolysis to promote cohesion, and condensation, which is suggested to proceed via formation of SMC rings, or assemblies. To learn more about the role of ATP in the architecture of, SMC proteins, we report crystal structures of nucleotide-free and ATP, bound P. furiosus SMC ATPase domains. ATP dimerizes two SMC ATPase domains, by binding to opposing Walker A and signature motifs, indicating that ATP, binding can directly assemble SMC proteins. DNA stimulates ATP hydrolysis, in the engaged SMC ABC domains, suggesting that ATP hydrolysis can be, allosterically regulated. Structural and mutagenesis data identify an SMC, protein conserved-arginine finger that is required for DNA stimulation of, the ATPase activity and directly connects a putative DNA interaction site, to ATP. Our results suggest that stimulation of the SMC ATPase activity, may be a specific feature to regulate the ATP-driven assembly and, disassembly of SMC proteins.
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<StructureSection load='1xew' size='340' side='right'caption='[[1xew]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xew]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XEW 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xew OCA], [https://pdbe.org/1xew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xew RCSB], [https://www.ebi.ac.uk/pdbsum/1xew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xew ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SMC_PYRFU SMC_PYRFU] Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.[HAMAP-Rule:MF_01894]
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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/xe/1xew_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=1xew 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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1XEW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XEW OCA].
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*[[Condensin|Condensin]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural biochemistry of ATP-driven dimerization and DNA-stimulated activation of SMC ATPases., Lammens A, Schele A, Hopfner KP, Curr Biol. 2004 Oct 5;14(19):1778-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15458651 15458651]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: Hopfner, K.P.]]
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[[Category: Hopfner K-P]]
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[[Category: Lammens, A.]]
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[[Category: Lammens A]]
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[[Category: Schele, A.]]
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[[Category: Schele A]]
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[[Category: abc-atpases]]
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[[Category: cohesin]]
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[[Category: condensin]]
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[[Category: smc]]
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[[Category: structural maintenance of chromosomes]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:01:06 2007''
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Current revision

Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.

PDB ID 1xew

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