1jg5: Difference between revisions

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<StructureSection load='1jg5' size='340' side='right'caption='[[1jg5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1jg5' size='340' side='right'caption='[[1jg5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1jg5]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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'>[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>
<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.  
[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]]
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</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=1jg5 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=1jg5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tetrahydrobiopterin, 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<ref>PMID:11580249</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jg5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Auerbach, G]]
[[Category: Rattus norvegicus]]
[[Category: Bacher, A]]
[[Category: Auerbach G]]
[[Category: Bader, G]]
[[Category: Bacher A]]
[[Category: Fischer, M]]
[[Category: Bader G]]
[[Category: Gutlich, M]]
[[Category: Fischer M]]
[[Category: Herrmann, A]]
[[Category: Gutlich M]]
[[Category: Huber, R]]
[[Category: Herrmann A]]
[[Category: Lemm, T]]
[[Category: Huber R]]
[[Category: Ploom, T]]
[[Category: Lemm T]]
[[Category: Schiffmann, S]]
[[Category: Ploom T]]
[[Category: Alpha/beta structure]]
[[Category: Schiffmann S]]
[[Category: Beta sheet]]
[[Category: Protein binding]]
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