1bxd: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BXD FirstGlance]. <br> | <table><tr><td colspan='2'>[[1bxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BXD FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=1bxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bxd RCSB], [http://www.ebi.ac.uk/pdbsum/1bxd 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=1bxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bxd RCSB], [http://www.ebi.ac.uk/pdbsum/1bxd 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Dutta, R | [[Category: Dutta, R]] | ||
[[Category: Ikura, M | [[Category: Ikura, M]] | ||
[[Category: Inouye, M | [[Category: Inouye, M]] | ||
[[Category: Ishima, R | [[Category: Ishima, R]] | ||
[[Category: Kainosho, M | [[Category: Kainosho, M]] | ||
[[Category: Liu, D | [[Category: Liu, D]] | ||
[[Category: Ono, A M | [[Category: Ono, A M]] | ||
[[Category: Park, H | [[Category: Park, H]] | ||
[[Category: Qin, L | [[Category: Qin, L]] | ||
[[Category: Saha, S K | [[Category: Saha, S K]] | ||
[[Category: Swindells, M B | [[Category: Swindells, M B]] | ||
[[Category: Tanaka, T | [[Category: Tanaka, T]] | ||
[[Category: Tomomori, C | [[Category: Tomomori, C]] | ||
[[Category: Tong, K I | [[Category: Tong, K I]] | ||
[[Category: Yamazaki, T | [[Category: Yamazaki, T]] | ||
[[Category: His-asp phosphorelay system]] | [[Category: His-asp phosphorelay system]] | ||
[[Category: Histidine kinase]] | [[Category: Histidine kinase]] | ||
Revision as of 14:45, 22 December 2014
NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZNMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ
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 PubMedBacteria live in capricious environments, in which they must continuously sense external conditions in order to adjust their shape, motility and physiology. The histidine-aspartate phosphorelay signal-transduction system (also known as the two-component system) is important in cellular adaptation to environmental changes in both prokaryotes and lower eukaryotes. In this system, protein histidine kinases function as sensors and signal transducers. The Escherichia coli osmosensor, EnvZ, is a transmembrane protein with histidine kinase activity in its cytoplasmic region. The cytoplasmic region contains two functional domains: domain A (residues 223-289) contains the conserved histidine residue (H243), a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR, whereas domain B (residues 290-450) encloses several highly conserved regions (G1, G2, F and N boxes) and is able to phosphorylate H243. Here we present the solution structure of domain B, the catalytic core of EnvZ. This core has a novel protein kinase structure, distinct from the serine/threonine/tyrosine kinase fold, with unanticipated similarities to both heatshock protein 90 and DNA gyrase B. NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ.,Tanaka T, Saha SK, Tomomori C, Ishima R, Liu D, Tong KI, Park H, Dutta R, Qin L, Swindells MB, Yamazaki T, Ono AM, Kainosho M, Inouye M, Ikura M Nature. 1998 Nov 5;396(6706):88-92. PMID:9817206[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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