2a0b

<StructureSection load='2a0b' size='340' side='right' caption='[[2a0b]], [[Resolution|resolution]] 1.57&Aring;' scene=''>

<table><tr><td colspan='2'>[[2a0b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A0B FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a0b OCA], [http://pdbe.org/2a0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a0b RCSB], [http://www.ebi.ac.uk/pdbsum/2a0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a0b ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ARCB_ECOLI ARCB_ECOLI]] Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576.

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== Publication Abstract from PubMed ==

The crystal structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli has been refined to 1.57 A resolution, using the coordinates of the earlier 2.06 A structure as a starting model. The final model contained 956 protein atoms, one zinc ion and 156 water molecules, with an R factor of 19.0%. The high-resolution electron-density maps clearly revealed additional solvent molecules and seven discrete rotamers in the protein side chains. One residue, Met755, was fully buried but was able to occupy the space in the hydrophobic core by means of the two-state conformation of its side chain. One water molecule was buried in the protein core and contributed to the rigidity of the HPt domain, cooperating in the coordination of the zinc ion.

Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution.,Kato M, Mizuno T, Shimizu T, Hakoshima T Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1842-9. PMID:10531481<ref>PMID:10531481</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2a0b" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Hakoshima, T]]

[[Category: Kato, M]]

[[Category: Mizuno, T]]

[[Category: Shimizu, T]]

[[Category: Two-component system]]