3pvs

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<StructureSection load='3pvs' size='340' side='right'caption='[[3pvs]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3pvs' size='340' side='right'caption='[[3pvs]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pvs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PVS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pvs]] is a 4 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=3PVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PVS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 2.5&#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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvs OCA], [https://pdbe.org/3pvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pvs RCSB], [https://www.ebi.ac.uk/pdbsum/3pvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pvs ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvs OCA], [https://pdbe.org/3pvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pvs RCSB], [https://www.ebi.ac.uk/pdbsum/3pvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pvs ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Bacterial "maintenance of genome stability protein A" (MgsA) and related eukaryotic enzymes play important roles in cellular responses to stalled DNA replication processes. Sequence information identifies MgsA enzymes as members of the clamp loader clade of AAA(+) proteins, but structural information defining the family has been limited. Here, the x-ray crystal structure of Escherichia coli MgsA is described, revealing a homotetrameric arrangement for the protein that distinguishes it from other clamp loader clade AAA(+) proteins. Each MgsA protomer is composed of three elements as follows: ATP-binding and helical lid domains (conserved among AAA(+) proteins) and a tetramerization domain. Although the tetramerization domains bury the greatest amount of surface area in the MgsA oligomer, each of the domains participates in oligomerization to form a highly intertwined quaternary structure. Phosphate is bound at each AAA(+) ATP-binding site, but the active sites do not appear to be in a catalytically competent conformation due to displacement of Arg finger residues. E. coli MgsA is also shown to form a complex with the single-stranded DNA-binding protein through co-purification and biochemical studies. MgsA DNA-dependent ATPase activity is inhibited by single-stranded DNA-binding protein. Together, these structural and biochemical observations provide insights into the mechanisms of MgsA family AAA(+) proteins.
 
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Structure and Biochemical Activities of Escherichia coli MgsA.,Page AN, George NP, Marceau AH, Cox MM, Keck JL J Biol Chem. 2011 Apr 8;286(14):12075-85. Epub 2011 Feb 5. PMID:21297161<ref>PMID:21297161</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 3pvs" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cox, M M]]
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[[Category: Cox MM]]
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[[Category: George, N P]]
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[[Category: George NP]]
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[[Category: Keck, J L]]
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[[Category: Keck JL]]
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[[Category: Marceau, A H]]
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[[Category: Marceau AH]]
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[[Category: Page, A N]]
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[[Category: Page AN]]
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[[Category: Maintenance of genome stability protein some]]
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[[Category: Recombination]]
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[[Category: Recombination protein some]]
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Current revision

Structure and biochemical activities of Escherichia coli MgsA

PDB ID 3pvs

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