4zms: Difference between revisions
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The | ==Structure of the full-length response regulator spr1814 in complex with a phosphate analogue and B3C== | ||
<StructureSection load='4zms' size='340' side='right' caption='[[4zms]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zms]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZMS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4QT:5-AMINO-2,4,6-TRIBROMOBENZENE-1,3-DIYL+DIHYDROPEROXIDE'>4QT</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zmr|4zmr]]</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=4zms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zms OCA], [http://pdbe.org/4zms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zms RCSB], [http://www.ebi.ac.uk/pdbsum/4zms PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3(-)) was determined at 2.0 A. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the alpha4-beta5-alpha5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain. | |||
Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region.,Park AK, Lee JH, Chi YM, Park H Biochem Biophys Res Commun. 2016 Apr 29;473(2):625-9. doi:, 10.1016/j.bbrc.2016.03.144. Epub 2016 Mar 30. PMID:27038544<ref>PMID:27038544</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 4zms" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chi, Y M]] | |||
[[Category: Park, A]] | [[Category: Park, A]] | ||
[[Category: | [[Category: Dna binding protein]] | ||
[[Category: Response regulator]] | |||
Revision as of 20:31, 10 May 2016
Structure of the full-length response regulator spr1814 in complex with a phosphate analogue and B3CStructure of the full-length response regulator spr1814 in complex with a phosphate analogue and B3C
Structural highlights
Publication Abstract from PubMedSpr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3(-)) was determined at 2.0 A. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the alpha4-beta5-alpha5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain. Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region.,Park AK, Lee JH, Chi YM, Park H Biochem Biophys Res Commun. 2016 Apr 29;473(2):625-9. doi:, 10.1016/j.bbrc.2016.03.144. Epub 2016 Mar 30. PMID:27038544[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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