1is8
From Proteopedia
(New page: 200px<br /><applet load="1is8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1is8, resolution 2.70Å" /> '''Crystal structure of...) |
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| - | [[Image:1is8.gif|left|200px]]<br /><applet load="1is8" size=" | + | [[Image:1is8.gif|left|200px]]<br /><applet load="1is8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1is8, resolution 2.70Å" /> | caption="1is8, resolution 2.70Å" /> | ||
'''Crystal structure of rat GTPCHI/GFRP stimulatory complex plus Zn'''<br /> | '''Crystal structure of rat GTPCHI/GFRP stimulatory complex plus Zn'''<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== | ||
| - | 1IS8 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, ZN 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:// | + | 1IS8 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>, <scene name='pdbligand=ZN:'>ZN</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=1IS8 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 13:15:15 2008'' |
Revision as of 11:15, 21 February 2008
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Crystal structure of rat GTPCHI/GFRP stimulatory complex plus Zn
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
1IS8 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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