2mda: Difference between revisions
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==The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase== | |||
<StructureSection load='2mda' size='340' side='right' caption='[[2mda]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mda]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MDA FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Th ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2mda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mda RCSB], [http://www.ebi.ac.uk/pdbsum/2mda PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/TY3H_RAT TY3H_RAT]] Plays an important role in the physiology of adrenergic neurons. | [[http://www.uniprot.org/uniprot/TY3H_RAT TY3H_RAT]] Plays an important role in the physiology of adrenergic neurons. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine in the biosynthesis of the catecholamine neurotransmitters. The activity of the enzyme is regulated by phosphorylation of serine residues in a regulatory domain and by binding of catecholamines to the active site. Available structures of TyrH lack the regulatory domain, limiting the understanding of the effect of regulation on structure. We report the use of NMR spectroscopy to analyze the solution structure of the isolated regulatory domain of rat TyrH. The protein is composed of a largely unstructured N-terminal region (residues 1-71) and a well-folded C-terminal portion (residues 72-159). The structure of a truncated version of the regulatory domain containing residues 65-159 has been determined and establishes that it is an ACT domain. The isolated domain is a homodimer in solution, with the structure of each monomer very similar to that of the core of the regulatory domain of phenylalanine hydroxylase. Two TyrH regulatory domain monomers form an ACT domain dimer composed of a sheet of eight strands with four alpha-helices on one side of the sheet. Backbone dynamic analyses were carried out to characterize the conformational flexibility of TyrH65-159. The results provide molecular details critical for understanding the regulatory mechanism of TyrH. | |||
The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase.,Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF J Mol Biol. 2013 Dec 17. pii: S0022-2836(13)00779-1. doi:, 10.1016/j.jmb.2013.12.015. PMID:24361276<ref>PMID:24361276</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Fitzpatrick, P | == References == | ||
[[Category: Hinck, A | <references/> | ||
[[Category: Huang, T | __TOC__ | ||
[[Category: Zhang, S | </StructureSection> | ||
[[Category: Buffalo rat]] | |||
[[Category: Fitzpatrick, P]] | |||
[[Category: Hinck, A]] | |||
[[Category: Huang, T]] | |||
[[Category: Zhang, S]] | |||
[[Category: Act domain]] | [[Category: Act domain]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Regulation]] | [[Category: Regulation]] | ||
[[Category: Tyrosine hydroxylase]] | [[Category: Tyrosine hydroxylase]] | ||
Revision as of 03:51, 25 December 2014
The Solution Structure of the Regulatory Domain of Tyrosine HydroxylaseThe Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase
Structural highlights
Function[TY3H_RAT] Plays an important role in the physiology of adrenergic neurons. Publication Abstract from PubMedTyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine in the biosynthesis of the catecholamine neurotransmitters. The activity of the enzyme is regulated by phosphorylation of serine residues in a regulatory domain and by binding of catecholamines to the active site. Available structures of TyrH lack the regulatory domain, limiting the understanding of the effect of regulation on structure. We report the use of NMR spectroscopy to analyze the solution structure of the isolated regulatory domain of rat TyrH. The protein is composed of a largely unstructured N-terminal region (residues 1-71) and a well-folded C-terminal portion (residues 72-159). The structure of a truncated version of the regulatory domain containing residues 65-159 has been determined and establishes that it is an ACT domain. The isolated domain is a homodimer in solution, with the structure of each monomer very similar to that of the core of the regulatory domain of phenylalanine hydroxylase. Two TyrH regulatory domain monomers form an ACT domain dimer composed of a sheet of eight strands with four alpha-helices on one side of the sheet. Backbone dynamic analyses were carried out to characterize the conformational flexibility of TyrH65-159. The results provide molecular details critical for understanding the regulatory mechanism of TyrH. The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase.,Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF J Mol Biol. 2013 Dec 17. pii: S0022-2836(13)00779-1. doi:, 10.1016/j.jmb.2013.12.015. PMID:24361276[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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