1a0b: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a0b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0B FirstGlance]. <br> | <table><tr><td colspan='2'>[[1a0b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0B FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | </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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0b RCSB], [http://www.ebi.ac.uk/pdbsum/1a0b PDBsum]</span></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=1a0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0b RCSB], [http://www.ebi.ac.uk/pdbsum/1a0b PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Hakoshima, T | [[Category: Hakoshima, T]] | ||
[[Category: Kato, M | [[Category: Kato, M]] | ||
[[Category: Mizuno, T | [[Category: Mizuno, T]] | ||
[[Category: Shimizu, T | [[Category: Shimizu, T]] | ||
[[Category: Four-helix bundle]] | [[Category: Four-helix bundle]] | ||
[[Category: Histidine kinase]] | [[Category: Histidine kinase]] | ||
[[Category: Phosphotransfer]] | [[Category: Phosphotransfer]] | ||
[[Category: Two-component system]] | [[Category: Two-component system]] | ||
Revision as of 14:08, 22 December 2014
HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLIHISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ARCB FROM ESCHERICHIA COLI
Structural highlights
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 PubMedThe histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined at 2.06 A resolution. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB.,Kato M, Mizuno T, Shimizu T, Hakoshima T Cell. 1997 Mar 7;88(5):717-23. PMID:9054511[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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