View source for 4rz2


==Crystal structure of the MinD-like ATPase FlhG==
<StructureSection load='4rz2' size='340' side='right'caption='[[4rz2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rz2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans_NG80-2 Geobacillus thermodenitrificans NG80-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RZ2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=4rz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rz2 OCA], [https://pdbe.org/4rz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rz2 RCSB], [https://www.ebi.ac.uk/pdbsum/4rz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rz2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4IMB4_GEOTN A4IMB4_GEOTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The number and location of flagella, bacterial organelles of locomotion, are species specific and appear in regular patterns that represent one of the earliest taxonomic criteria in microbiology. However, the mechanisms that reproducibly establish these patterns during each round of cell division are poorly understood. FlhG (previously YlxH) is a major determinant for a variety of flagellation patterns. Here, we show that FlhG is a structural homolog of the ATPase MinD, which serves in cell-division site determination. Like MinD, FlhG forms homodimers that are dependent on ATP and lipids. It interacts with a complex of the flagellar C-ring proteins FliM and FliY (also FliN) in the Gram-positive, peritrichous-flagellated Bacillus subtilis and the Gram-negative, polar-flagellated Shewanella putrefaciens. FlhG interacts with FliM/FliY in a nucleotide-independent manner and activates FliM/FliY to assemble with the C-ring protein FliG in vitro. FlhG-driven assembly of the FliM/FliY/FliG complex is strongly enhanced by ATP and lipids. The protein shows a highly dynamic subcellular distribution between cytoplasm and flagellar basal bodies, suggesting that FlhG effects flagellar location and number during assembly of the C-ring. We describe the molecular evolution of a MinD-like ATPase into a flagellation pattern effector and suggest that the underappreciated structural diversity of the C-ring proteins might contribute to the formation of different flagellation patterns.

MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.,Schuhmacher JS, Rossmann F, Dempwolff F, Knauer C, Altegoer F, Steinchen W, Dorrich AK, Klingl A, Stephan M, Linne U, Thormann KM, Bange G Proc Natl Acad Sci U S A. 2015 Mar 10;112(10):3092-7. doi:, 10.1073/pnas.1419388112. Epub 2015 Mar 2. PMID:25733861<ref>PMID:25733861</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rz2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus thermodenitrificans NG80-2]]
[[Category: Large Structures]]
[[Category: Bange G]]
[[Category: Schuhmacher JS]]