1jg5: Difference between revisions
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<StructureSection load='1jg5' size='340' side='right'caption='[[1jg5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1jg5' size='340' side='right'caption='[[1jg5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jg5]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1jg5]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JG5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jg5 OCA], [https://pdbe.org/1jg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jg5 RCSB], [https://www.ebi.ac.uk/pdbsum/1jg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jg5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/GFRP_RAT GFRP_RAT]] Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:40, 11 August 2021
CRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN, GFRPCRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN, GFRP
Structural highlights
Function[GFRP_RAT] Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine. 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 PubMedTetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids regulates its own synthesis in mammals through feedback inhibition of GTP cyclohydrolase I. This mechanism is mediated by a regulatory subunit called GTP cyclohydrolase I feedback regulatory protein (GFRP). The 2.6 A resolution crystal structure of rat GFRP shows that the protein forms a pentamer. This indicates a model for the interaction of mammalian GTP cyclohydrolase I with its regulator, GFRP. Kinetic investigations of human GTP cyclohydrolase I in complex with rat and human GFRP showed similar regulatory effects of both GFRP proteins. Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP.,Bader G, Schiffmann S, Herrmann A, Fischer M, Gutlich M, Auerbach G, Ploom T, Bacher A, Huber R, Lemm T J Mol Biol. 2001 Oct 5;312(5):1051-7. PMID:11580249[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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