Sandbox1qu7

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Once the <scene name='78/782579/Ligandalpha/2'>ligand</scene> binds to the periplasmic domain, it causes changes in the dynamics of the chemoreceptor. In the kinase-off state, the HAMP domain becomes<scene name='78/782579/Ligandhamp/1'> less flexible</scene>, the methylation sites become <scene name='78/782579/Ligandcyto/1'>more flexible</scene> and the cytoplasmic domain becomes less flexible.
Once the <scene name='78/782579/Ligandalpha/2'>ligand</scene> binds to the periplasmic domain, it causes changes in the dynamics of the chemoreceptor. In the kinase-off state, the HAMP domain becomes<scene name='78/782579/Ligandhamp/1'> less flexible</scene>, the methylation sites become <scene name='78/782579/Ligandcyto/1'>more flexible</scene> and the cytoplasmic domain becomes less flexible.
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To test the effects of changes to residues in the HAMP domain in the Tsr Receptor, certain residues were mutated. So codon-by-codon mutagenesis was performed on the regions <scene name='78/782579/Mutantsas1/1'>K215-A233</scene> in AS1 and E248-R265 in AS2. 13 of the mutant amino acids were considered either critical or important. Important residues are those residues at which a majority of amino acid replacements demonstrably impaired Tsr function. Critical residues are the ones at which majority of the deleterious replacements produced a complete loss-of-function (null) phenotype. By these criteria, AS1 has one important (P221) and six critical (L218, M222, L225, I229, I232, A233) residues; AS2 has six critical residues (E248, M249, L252, L256, M259, L263).
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To test the effects of changes to residues in the HAMP domain in the Tsr Receptor, certain residues were mutated. So codon-by-codon mutagenesis was performed on the regions <scene name='78/782579/Mutantsas1/3'>K215-A233</scene> in AS1 and E248-R265 in AS2. 13 of the mutant amino acids were considered either critical or important. Important residues are those residues at which a majority of amino acid replacements demonstrably impaired Tsr function. Critical residues are the ones at which majority of the deleterious replacements produced a complete loss-of-function (null) phenotype. By these criteria, AS1 has one important (P221) and six critical (L218, M222, L225, I229, I232, A233) residues; AS2 has six critical residues (E248, M249, L252, L256, M259, L263).

Revision as of 16:24, 20 April 2018

This the structure of Ser Protein which is a chemoreceptor, this forms a trimer of dimers

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 Parkinson JS, Hazelbauer GL, Falke JJ. Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update. Trends Microbiol. 2015 May;23(5):257-66. doi: 10.1016/j.tim.2015.03.003. Epub, 2015 Mar 30. PMID:25834953 doi:http://dx.doi.org/10.1016/j.tim.2015.03.003
  2. ↑ Harris MJ, Struppe JO, Wylie BJ, McDermott AE, Thompson LK. Multidimensional Solid-State Nuclear Magnetic Resonance of a Functional Multiprotein Chemoreceptor Array. Biochemistry. 2016 Jul 5;55(26):3616-24. doi: 10.1021/acs.biochem.6b00234. Epub, 2016 Jun 24. PMID:27295350 doi:http://dx.doi.org/10.1021/acs.biochem.6b00234
  3. ↑ Swain KE, Gonzalez MA, Falke JJ. Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor. Biochemistry. 2009 Oct 6;48(39):9266-77. PMID:19705835 doi:http://dx.doi.org/10.1021/bi901020d
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