View source for 5cj9


==Bacillus halodurans Arginine repressor, ArgR==
<StructureSection load='5cj9' size='340' side='right'caption='[[5cj9]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cj9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CJ9 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]] 2.409&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></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=5cj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cj9 OCA], [https://pdbe.org/5cj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cj9 RCSB], [https://www.ebi.ac.uk/pdbsum/5cj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cj9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARGR_HALH5 ARGR_HALH5] Regulates arginine biosynthesis genes.[HAMAP-Rule:MF_00173]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The arginine repressor (ArgR) is an arginine-dependent transcription factor that regulates the expression of genes encoding proteins involved in the arginine biosynthesis and catabolic pathways. ArgR is a functional homolog of the arginine-dependent repressor/activator AhrC from Bacillus subtilis, and belongs to the ArgR/AhrC family of transcriptional regulators. In this research, we determined the structure of the ArgR (Bh2777) from Bacillus halodurans at 2.41 A resolution by X-ray crystallography. The ArgR from B. halodurans appeared to be a trimer in a size exclusion column and in the crystal structure. However, it formed a hexamer in the presence of L-arginine in multi-angle light scattering (MALS) studies, indicating the oligomerization state was dependent on the presence of L-arginine. The trimeric structure showed that the C-terminal domains form the core, which was made by inter-subunit interactions mainly through hydrophobic contacts, while the N-terminal domains containing a winged helix-turn-helix DNA binding motif were arranged around the periphery. The arrangement of trimeric structure in the B. halodurans ArgR was different from those of other ArgR homologs previously reported. We finally showed that the B. halodurans ArgR has an arginine-dependent DNA binding property by an electrophoretic mobility shift assay.

Structural Analysis and Insights into the Oligomeric State of an Arginine-Dependent Transcriptional Regulator from Bacillus halodurans.,Park YW, Kang J, Yeo HK, Lee JY PLoS One. 2016 May 12;11(5):e0155396. doi: 10.1371/journal.pone.0155396., eCollection 2016. PMID:27171430<ref>PMID:27171430</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cj9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Arginine repressor 3D structures|Arginine repressor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alkalihalobacillus halodurans C-125]]
[[Category: Large Structures]]
[[Category: Kang J]]
[[Category: Lee JY]]
[[Category: Park YW]]
[[Category: Yeo HY]]