2lfs: Difference between revisions
No edit summary |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant== | ||
<StructureSection load='2lfs' size='340' side='right'caption='[[2lfs]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lfs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LFS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lfs OCA], [https://pdbe.org/2lfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lfs RCSB], [https://www.ebi.ac.uk/pdbsum/2lfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lfs ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ENVZ_SHIFL ENVZ_SHIFL] 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 (By similarity). This two-component system plays a role in virulence (By similarity).[UniProtKB:A0A4P7TSF2][UniProtKB:P0AEJ4][https://www.uniprot.org/uniprot/O28769_ARCFU O28769_ARCFU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity. | |||
Mechanism of regulation of receptor histidine kinases.,Ferris HU, Dunin-Horkawicz S, Hornig N, Hulko M, Martin J, Schultz JE, Zeth K, Lupas AN, Coles M Structure. 2012 Jan 11;20(1):56-66. PMID:22244755<ref>PMID:22244755</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lfs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Archaeoglobus fulgidus DSM 4304]] | ||
[[Category: Large Structures]] | |||
[[Category: Shigella flexneri]] | |||
== | [[Category: Coles M]] | ||
< | [[Category: Ferris HU]] | ||
[[Category: Archaeoglobus fulgidus | [[Category: Hulko M]] | ||
[[Category: | [[Category: Lupas AN]] | ||
[[Category: Coles | [[Category: Martin J]] | ||
[[Category: Ferris | |||
[[Category: Hulko | |||
[[Category: Lupas | |||
[[Category: Martin | |||
Latest revision as of 08:42, 15 May 2024
Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variantSolution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant
Structural highlights
FunctionENVZ_SHIFL 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 (By similarity). This two-component system plays a role in virulence (By similarity).[UniProtKB:A0A4P7TSF2][UniProtKB:P0AEJ4]O28769_ARCFU Publication Abstract from PubMedBacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity. Mechanism of regulation of receptor histidine kinases.,Ferris HU, Dunin-Horkawicz S, Hornig N, Hulko M, Martin J, Schultz JE, Zeth K, Lupas AN, Coles M Structure. 2012 Jan 11;20(1):56-66. PMID:22244755[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||