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| | <StructureSection load='1ion' size='340' side='right'caption='[[1ion]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1ion' size='340' side='right'caption='[[1ion]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ion]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1ION FirstGlance]. <br> | + | <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> |
| - | </td></tr><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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MIND-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ion FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ion OCA], [http://pdbe.org/1ion PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ion RCSB], [http://www.ebi.ac.uk/pdbsum/1ion PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ion ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O58346_PYRHO O58346_PYRHO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1ion" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1ion" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[User:Eric Martz/Entertaining PDB codes|User:Eric Martz/Entertaining PDB codes]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyrococcus horikoshii]] | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Itou, H]] | + | [[Category: Itou H]] |
| - | [[Category: Sakai, N]] | + | [[Category: Sakai N]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Tanaka I]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Tanokura M]] |
| - | [[Category: Watanabe, N]] | + | [[Category: Watanabe N]] |
| - | [[Category: Yao, M]] | + | [[Category: Yao M]] |
| - | [[Category: Yumoto, F]] | + | [[Category: Yumoto F]] |
| - | [[Category: Adp-binding protein]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division inhibitor]]
| + | |
| - | [[Category: Mind]]
| + | |
| - | [[Category: P-loop]]
| + | |
| Structural highlights
Function
O58346_PYRHO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sakai N, Yao M, Itou H, Watanabe N, Yumoto F, Tanokura M, Tanaka I. The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP. Structure. 2001 Sep;9(9):817-26. PMID:11566131
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