2xit: Difference between revisions

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-[[Image:2xit.png|left|200px]]
+==Crystal structure of monomeric MipZ==
+<StructureSection load='2xit' size='340' side='right' caption='[[2xit]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2xit]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XIT OCA]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xj4|2xj4]], [[2xj9|2xj9]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xit RCSB], [http://www.ebi.ac.uk/pdbsum/2xit PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein gradients play a central role in the spatial organization of cells, but the mechanisms of their formation are incompletely understood. This study analyzes the determinants responsible for establishing bipolar gradients of the ATPase MipZ, a key regulator of division site placement in Caulobacter crescentus. We have solved the crystal structure of MipZ in different nucleotide states, dissected its ATPase cycle, and investigated its interaction with FtsZ, ParB, and the nucleoid. Our results suggest that the polar ParB complexes locally stimulate the formation of ATP-bound MipZ dimers, which are then retained near the cell poles through association with chromosomal DNA. Due to their intrinsic ATPase activity, dimers eventually dissociate into freely diffusible monomers that undergo spontaneous nucleotide exchange and are recaptured by ParB. These findings clarify the molecular function of a conserved gradient-forming system and reveal mechanistic principles that might be commonly used to sustain protein gradients within cells.
-<!--
+Localized Dimerization and Nucleoid Binding Drive Gradient Formation by the Bacterial Cell Division Inhibitor MipZ.,Kiekebusch D, Michie KA, Essen LO, Lowe J, Thanbichler M Mol Cell. 2012 May 11;46(3):245-59. Epub 2012 Apr 5. PMID:22483621<ref>PMID:22483621</ref>
-The line below this paragraph, containing "STRUCTURE_2xit", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2xit|  PDB=2xit  |  SCENE=  }}
-===Crystal structure of monomeric MipZ===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_22483621}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 22483621 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_22483621}}
-==About this Structure==
-[[2xit]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XIT OCA].
-==Reference==
-<ref group="xtra">PMID:022483621</ref><references group="xtra"/>
 [[Category: Caulobacter vibrioides]]
 [[Category: Essen, L O.]]