1b4a: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1b4a]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B4A FirstGlance]. <br>
<table><tr><td colspan='2'>[[1b4a]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B4A FirstGlance]. <br>
</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=1b4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4a OCA], [https://pdbe.org/1b4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b4a RCSB], [https://www.ebi.ac.uk/pdbsum/1b4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b4a ProSAT]</span></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]] 2.5&#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=1b4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4a OCA], [https://pdbe.org/1b4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b4a RCSB], [https://www.ebi.ac.uk/pdbsum/1b4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b4a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ARGR_GEOSE ARGR_GEOSE]] Regulates arginine biosynthesis genes.  
[https://www.uniprot.org/uniprot/ARGR_GEOSE ARGR_GEOSE] Regulates arginine biosynthesis genes.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Charlier, D]]
[[Category: Charlier D]]
[[Category: Duyne, G D.Van]]
[[Category: Glansdorff N]]
[[Category: Glansdorff, N]]
[[Category: Ni J]]
[[Category: Ni, J]]
[[Category: Sakanyan V]]
[[Category: Sakanyan, V]]
[[Category: Van Duyne GD]]
[[Category: Arginine]]
[[Category: Helix turn helix]]
[[Category: Repressor]]

Latest revision as of 13:58, 2 August 2023

STRUCTURE OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUSSTRUCTURE OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS

Structural highlights

1b4a is a 6 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARGR_GEOSE Regulates arginine biosynthesis genes.

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

The arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here, we present the 2.5 A structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 A structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits, with six DNA-binding domains surrounding a central oligomeric core. The difference in quaternary organization of subunits in the arginine-bound and apo forms provides a possible explanation for poor operator binding by apo-ArgR and for high affinity binding in the presence of arginine.

Structure of the arginine repressor from Bacillus stearothermophilus.,Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD. Structure of the arginine repressor from Bacillus stearothermophilus. Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868 doi:http://dx.doi.org/10.1038/8229

1b4a, resolution 2.50Å

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