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1ion

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(New page: 200px<br /><applet load="1ion" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ion, resolution 2.30&Aring;" /> '''THE SEPTUM SITE-DETE...)
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[[Image:1ion.gif|left|200px]]<br /><applet load="1ion" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ion, resolution 2.30&Aring;" />
 
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'''THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3'''<br />
 
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==Overview==
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==THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3==
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BACKGROUND: In Escherichia coli, the cell division site is determined by, the cooperative activity of min operon products MinC, MinD, and MinE. MinC, is a nonspecific inhibitor of the septum protein FtsZ, and MinE is the, supressor of MinC. MinD plays a multifunctional role. It is a, membrane-associated ATPase and is a septum site-determining factor through, the activation and regulation of MinC and MinE. MinD is also known to, undergo a rapid pole-to-pole oscillation movement in vivo as observed by, fluorescent microscopy. RESULTS: The three-dimensional structure of the, MinD-2 from Pyrococcus horikoshii OT3 (PH0612) has been determined at 2.3, A resolution by X-ray crystallography using the Se-Met MAD method. The, molecule consists of a beta sheet with 7 parallel and 1 antiparallel, strands and 11 peripheral alpha helices. It contains the classical, mononucleotide binding loop with bound ADP and magnesium ion, which is, consistent with the suggested ATPase activity. CONCLUSIONS: Structure, analysis shows that MinD is most similar to nitrogenase iron protein, which is a member of the P loop-containing nucleotide triphosphate, hydrolase superfamily of proteins. Unlike nitrogenase or other member, proteins that normally work as a dimer, MinD was present as a monomer in, the crystal. Both the 31P NMR and Malachite Green method exhibited, relatively low levels of ATPase activity. These facts suggest that MinD, may work as a molecular switch in the multiprotein complex in bacterial, cell division.
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<StructureSection load='1ion' size='340' side='right'caption='[[1ion]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ion]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ION OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ION 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]] 2.3&#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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1ion FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ion OCA], [https://pdbe.org/1ion PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ion RCSB], [https://www.ebi.ac.uk/pdbsum/1ion PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ion ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O58346_PYRHO O58346_PYRHO]
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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/io/1ion_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=1ion 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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BACKGROUND: In Escherichia coli, the cell division site is determined by the cooperative activity of min operon products MinC, MinD, and MinE. MinC is a nonspecific inhibitor of the septum protein FtsZ, and MinE is the supressor of MinC. MinD plays a multifunctional role. It is a membrane-associated ATPase and is a septum site-determining factor through the activation and regulation of MinC and MinE. MinD is also known to undergo a rapid pole-to-pole oscillation movement in vivo as observed by fluorescent microscopy. RESULTS: The three-dimensional structure of the MinD-2 from Pyrococcus horikoshii OT3 (PH0612) has been determined at 2.3 A resolution by X-ray crystallography using the Se-Met MAD method. The molecule consists of a beta sheet with 7 parallel and 1 antiparallel strands and 11 peripheral alpha helices. It contains the classical mononucleotide binding loop with bound ADP and magnesium ion, which is consistent with the suggested ATPase activity. CONCLUSIONS: Structure analysis shows that MinD is most similar to nitrogenase iron protein, which is a member of the P loop-containing nucleotide triphosphate hydrolase superfamily of proteins. Unlike nitrogenase or other member proteins that normally work as a dimer, MinD was present as a monomer in the crystal. Both the 31P NMR and Malachite Green method exhibited relatively low levels of ATPase activity. These facts suggest that MinD may work as a molecular switch in the multiprotein complex in bacterial cell division.
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==About this Structure==
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The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP.,Sakai N, Yao M, Itou H, Watanabe N, Yumoto F, Tanokura M, Tanaka I Structure. 2001 Sep;9(9):817-26. PMID:11566131<ref>PMID:11566131</ref>
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1ION is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ION OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP., Sakai N, Yao M, Itou H, Watanabe N, Yumoto F, Tanokura M, Tanaka I, Structure. 2001 Sep;9(9):817-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11566131 11566131]
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</div>
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[[Category: Pyrococcus horikoshii]]
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<div class="pdbe-citations 1ion" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Itou, H.]]
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<references/>
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[[Category: Sakai, N.]]
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__TOC__
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[[Category: Tanaka, I.]]
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</StructureSection>
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[[Category: Tanokura, M.]]
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[[Category: Large Structures]]
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[[Category: Watanabe, N.]]
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[[Category: Pyrococcus horikoshii OT3]]
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[[Category: Yao, M.]]
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[[Category: Itou H]]
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[[Category: Yumoto, F.]]
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[[Category: Sakai N]]
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[[Category: ADP]]
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[[Category: Tanaka I]]
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[[Category: MG]]
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[[Category: Tanokura M]]
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[[Category: adp-binding protein]]
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[[Category: Watanabe N]]
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[[Category: cell division inhibitor]]
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[[Category: Yao M]]
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[[Category: mind]]
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[[Category: Yumoto F]]
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[[Category: p-loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:18:38 2007''
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Current revision

THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3

PDB ID 1ion

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