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1bxd

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Revision as of 06:17, 17 August 2017

NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ

Structural highlights

1bxd is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ENVZ_ECOLI] Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals.

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

Bacteria 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

↑ 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. NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ. Nature. 1998 Nov 5;396(6706):88-92. PMID:9817206 doi:http://dx.doi.org/10.1038/23968

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bxd"

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ==
 <StructureSection load='1bxd' size='340' side='right' caption='[[1bxd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. 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. 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 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 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://pdbe.org/1bxd PDBe], [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://pdbe.org/1bxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bxd RCSB], [http://www.ebi.ac.uk/pdbsum/1bxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bxd ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Ecobd]]
 [[Category: Dutta, R]]
 [[Category: Ikura, M]]

1bxd

From Proteopedia

Revision as of 06:17, 17 August 2017

NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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