1is7: Difference between revisions

Revision as of 13:54, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1is7.png

Template:STRUCTURE 1is7

Crystal structure of rat GTPCHI/GFRP stimulatory complexCrystal structure of rat GTPCHI/GFRP stimulatory complex

Template:ABSTRACT PUBMED 11818540

About this StructureAbout this Structure

1IS7 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP., Maita N, Okada K, Hatakeyama K, Hakoshima T, Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1212-7. Epub 2002 Jan 29. PMID:11818540

Page seeded by OCA on Tue Jul 1 13:54:44 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1is7.gif|left|200px]]
+{{Seed}}
+[[Image:1is7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1is7|  PDB=1is7  |  SCENE=  }}
-'''Crystal structure of rat GTPCHI/GFRP stimulatory complex'''
+===Crystal structure of rat GTPCHI/GFRP stimulatory complex===
-==Overview==
+<!--
-In the presence of phenylalanine, GTP cyclohydrolase I feedback regulatory protein (GFRP) forms a stimulatory 360-kDa complex with GTP cyclohydrolase I (GTPCHI), which is the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin. The crystal structure of the stimulatory complex reveals that the GTPCHI decamer is sandwiched by two GFRP homopentamers. Each GFRP pentamer forms a symmetrical five-membered ring similar to beta-propeller. Five phenylalanine molecules are buried inside each interface between GFRP and GTPCHI, thus enhancing the binding of these proteins. The complex structure suggests that phenylalanine-induced GTPCHI x GFRP complex formation enhances GTPCHI activity by locking the enzyme in the active state.
+The line below this paragraph, {{ABSTRACT_PUBMED_11818540}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11818540 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11818540}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Okada, K.]]
 [[Category: Enzyme-regulatory protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:21:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 13:54:44 2008''