1is7
From Proteopedia
(New page: 200px<br /><applet load="1is7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1is7, resolution 2.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1is7.gif|left|200px]]<br /><applet load="1is7" size=" | + | [[Image:1is7.gif|left|200px]]<br /><applet load="1is7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1is7, resolution 2.8Å" /> | caption="1is7, resolution 2.8Å" /> | ||
'''Crystal structure of rat GTPCHI/GFRP stimulatory complex'''<br /> | '''Crystal structure of rat GTPCHI/GFRP stimulatory complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the presence of phenylalanine, GTP cyclohydrolase I feedback regulatory | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1IS7 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 K and PHE 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:// | + | 1IS7 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=K:'>K</scene> and <scene name='pdbligand=PHE:'>PHE</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=1IS7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: enzyme-regulatory protein complex]] | [[Category: enzyme-regulatory protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:04 2008'' |
Revision as of 11:15, 21 February 2008
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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.
About this Structure
1IS7 is a Protein complex structure of sequences from Rattus norvegicus with and as ligands. Active as GTP cyclohydrolase I, with EC number 3.5.4.16 Full crystallographic information is available from OCA.
Reference
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
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