1wpl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wpl.gif|left|200px]]<br /><applet load="1wpl" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1wpl.gif|left|200px]]
-
caption="1wpl, resolution 2.8&Aring;" />
+
 
-
'''Crystal structure of the inhibitory form of rat GTP cyclohydrolase I/GFRP complex'''<br />
+
{{Structure
 +
|PDB= 1wpl |SIZE=350|CAPTION= <scene name='initialview01'>1wpl</scene>, resolution 2.8&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene> and <scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of the inhibitory form of rat GTP cyclohydrolase I/GFRP complex'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1WPL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HBI:'>HBI</scene> and <scene name='pdbligand=3PO:'>3PO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPL OCA].
+
1WPL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPL OCA].
==Reference==
==Reference==
-
Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein., Maita N, Hatakeyama K, Okada K, Hakoshima T, J Biol Chem. 2004 Dec 3;279(49):51534-40. Epub 2004 Sep 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15448133 15448133]
+
Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein., Maita N, Hatakeyama K, Okada K, Hakoshima T, J Biol Chem. 2004 Dec 3;279(49):51534-40. Epub 2004 Sep 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15448133 15448133]
[[Category: GTP cyclohydrolase I]]
[[Category: GTP cyclohydrolase I]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 24: Line 33:
[[Category: enzyme-regulatory protein complex]]
[[Category: enzyme-regulatory protein complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:50 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:02 2008''

Revision as of 13:00, 20 March 2008


PDB ID 1wpl

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: , , and
Activity: GTP cyclohydrolase I, with EC number 3.5.4.16
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the inhibitory form of rat GTP cyclohydrolase I/GFRP complex


Overview

GTP cyclohydrolase I (GTPCHI) is the rate-limiting enzyme involved in the biosynthesis of tetrahydrobiopterin, a key cofactor necessary for nitric oxide synthase and for the hydroxylases that are involved in the production of catecholamines and serotonin. In animals, the GTPCHI feedback regulatory protein (GFRP) binds GTPCHI to mediate feed-forward activation of GTPCHI activity in the presence of phenylalanine, whereas it induces feedback inhibition of enzyme activity in the presence of biopterin. Here, we have reported the crystal structure of the biopterin-induced inhibitory complex of GTPCHI and GFRP and compared it with the previously reported phenylalanine-induced stimulatory complex. The structure reveals five biopterin molecules located at each interface between GTPCHI and GFRP. Induced fitting structural changes by the biopterin binding expand large conformational changes in GTPCHI peptide segments forming the active site, resulting in inhibition of the activity. By locating 3,4-dihydroxy-phenylalanine-responsive dystonia mutations in the complex structure, we found mutations that may possibly disturb the GFRP-mediated regulation of GTPCHI.

About this Structure

1WPL is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein., Maita N, Hatakeyama K, Okada K, Hakoshima T, J Biol Chem. 2004 Dec 3;279(49):51534-40. Epub 2004 Sep 23. PMID:15448133

Page seeded by OCA on Thu Mar 20 15:00:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools