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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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"><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='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=1jg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jg5 OCA], [http://pdbe.org/1jg5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jg5 RCSB], [http://www.ebi.ac.uk/pdbsum/1jg5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jg5 ProSAT]</span></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>
</table>
</table>
== Function ==
== Function ==
[[http://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]]

Latest revision as of 16:24, 13 March 2024

CRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN, GFRPCRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN, GFRP

Structural highlights

1jg5 is a 5 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

1jg5, resolution 2.60Å

Drag the structure with the mouse to rotate

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OCA
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