View source for 6m10


==Crystal structure of PA4853 (Fis) from Pseudomonas aeruginosa==
<StructureSection load='6m10' size='340' side='right'caption='[[6m10]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6m10]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M10 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]] 2.985&#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=6m10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m10 OCA], [https://pdbe.org/6m10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m10 RCSB], [https://www.ebi.ac.uk/pdbsum/6m10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m10 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FISL_PSEAE FISL_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Factor for inversion stimulation (Fis) is a versatile bacterial nucleoid-associated protein that can directly bind and bend DNA to influence DNA topology. It also plays crucial roles in regulating bacterial virulence factors and in optimizing bacterial adaptation to various environments. Fis from Pseudomonas aeruginosa (PA4853, referred to as PaFis) has recently been found to be required for virulence by regulating the expression of type III secretion system (T3SS) genes. PaFis can specifically bind to the promoter region of exsA, which functions as a T3SS master regulator, to regulate its expression and plays an essential role in transcription elongation from exsB to exsA. Here, the crystal structure of PaFis, which is composed of a four-helix bundle and forms a homodimer, is reported. PaFis shows remarkable structural similarities to the well studied Escherichia coli Fis (EcFis), including an N-terminal flexible loop and a C-terminal helix-turn-helix (HTH) motif. However, the critical residues for Hin-catalyzed DNA inversion in the N-terminal loop of EcFis are not conserved in PaFis and further studies are required to investigate its exact role. A gel-electrophoresis mobility-shift assay showed that PaFis can efficiently bind to the promoter region of exsA. Structure-based mutagenesis revealed that several conserved basic residues in the HTH motif play essential roles in DNA binding. These structural and biochemical studies may help in understanding the role of PaFis in the regulation of T3SS expression and in virulence.

Crystal structure of the nucleoid-associated protein Fis (PA4853) from Pseudomonas aeruginosa.,Zhou J, Gao Z, Zhang H, Dong Y Acta Crystallogr F Struct Biol Commun. 2020 May 1;76(Pt 5):209-215. doi:, 10.1107/S2053230X20005427. Epub 2020 Apr 29. PMID:32356522<ref>PMID:32356522</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6m10" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Dong Y]]
[[Category: Gao Z]]
[[Category: Zhang H]]
[[Category: Zhou J]]