1mmi

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[[Image:1mmi.gif|left|200px]]
 
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{{Structure
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==E. COLI DNA POLYMERASE BETA SUBUNIT==
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|PDB= 1mmi |SIZE=350|CAPTION= <scene name='initialview01'>1mmi</scene>, resolution 1.848&Aring;
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<StructureSection load='1mmi' size='340' side='right'caption='[[1mmi]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1mmi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMI FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span>
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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]] 1.848&#8491;</td></tr>
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|GENE= dnaN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=1mmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmi OCA], [https://pdbe.org/1mmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmi RCSB], [https://www.ebi.ac.uk/pdbsum/1mmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmi ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[2pol|2POL]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmi OCA], [http://www.ebi.ac.uk/pdbsum/1mmi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mmi RCSB]</span>
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[https://www.uniprot.org/uniprot/DPO3B_ECOLI DPO3B_ECOLI] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA.
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}}
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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/mm/1mmi_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=1mmi ConSurf].
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<div style="clear:both"></div>
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'''E. COLI DNA POLYMERASE BETA SUBUNIT'''
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The beta subunit of the Escherichia coli replicative DNA polymerase III holoenzyme is the sliding clamp that interacts with the alpha (polymerase) subunit to maintain the high processivity of the enzyme. The beta protein is a ring-shaped dimer of 40.6 kDa subunits whose structure has previously been determined at a resolution of 2.5 A [Kong et al. (1992), Cell, 69, 425-437]. Here, the construction of a new plasmid that directs overproduction of beta to very high levels and a simple procedure for large-scale purification of the protein are described. Crystals grown under slightly modified conditions diffracted to beyond 1.9 A at 100 K at a synchrotron source. The structure of the beta dimer solved at 1.85 A resolution shows some differences from that reported previously. In particular, it was possible at this resolution to identify residues that differed in position between the two subunits in the unit cell; side chains of these and some other residues were found to occupy alternate conformations. This suggests that these residues are likely to be relatively mobile in solution. Some implications of this flexibility for the function of beta are discussed.
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==About this Structure==
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1MMI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMI OCA].
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==Reference==
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Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III., Oakley AJ, Prosselkov P, Wijffels G, Beck JL, Wilce MC, Dixon NE, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1192-9. Epub 2003, Jun 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12832762 12832762]
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[[Category: DNA-directed DNA polymerase]]
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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: Beck, J L.]]
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[[Category: Beck JL]]
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[[Category: Dixon, N E.]]
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[[Category: Dixon NE]]
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[[Category: Oakley, A J.]]
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[[Category: Oakley AJ]]
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[[Category: Prosselkov, P.]]
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[[Category: Prosselkov P]]
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[[Category: Wijffels, G.]]
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[[Category: Wijffels G]]
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[[Category: Wilce, M C.J.]]
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[[Category: Wilce MCJ]]
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[[Category: dna polymerase beta subunit]]
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[[Category: dna replication]]
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[[Category: e. coli]]
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[[Category: processivity factor]]
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[[Category: sliding clamp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:03 2008''
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Current revision

E. COLI DNA POLYMERASE BETA SUBUNIT

PDB ID 1mmi

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