1vcm
From Proteopedia
(New page: 200px<br /><applet load="1vcm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vcm, resolution 2.35Å" /> '''Crystal Structure of...) |
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| - | [[Image:1vcm.gif|left|200px]]<br /><applet load="1vcm" size=" | + | [[Image:1vcm.gif|left|200px]]<br /><applet load="1vcm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vcm, resolution 2.35Å" /> | caption="1vcm, resolution 2.35Å" /> | ||
'''Crystal Structure of T.th. HB8 CTP synthetase'''<br /> | '''Crystal Structure of T.th. HB8 CTP synthetase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CTP synthetase (CTPs) catalyzes the last step in CTP biosynthesis, in | + | CTP synthetase (CTPs) catalyzes the last step in CTP biosynthesis, in which ammonia generated at the glutaminase domain reacts with the ATP-phosphorylated UTP at the synthetase domain to give CTP. Glutamine hydrolysis is active in the presence of ATP and UTP and is stimulated by the addition of GTP. We report the crystal structures of Thermus thermophilus HB8 CTPs alone, CTPs with 3SO4(2-), and CTPs with glutamine. The enzyme is folded into a homotetramer with a cross-shaped structure. Based on the binding mode of sulfate anions to the synthetase site, ATP and UTP are computer modeled into CTPs with a geometry favorable for the reaction. Glutamine bound to the glutaminase domain is situated next to the triad of Glu-His-Cys as a catalyst and a water molecule. Structural information provides an insight into the conformational changes associated with the binding of ATP and UTP and the formation of the GTP binding site. |
==About this Structure== | ==About this Structure== | ||
| - | 1VCM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/CTP_synthase CTP synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] Full crystallographic information is available from [http:// | + | 1VCM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/CTP_synthase CTP synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Goto, M.]] | [[Category: Goto, M.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:57 2008'' |
Revision as of 13:33, 21 February 2008
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Crystal Structure of T.th. HB8 CTP synthetase
Overview
CTP synthetase (CTPs) catalyzes the last step in CTP biosynthesis, in which ammonia generated at the glutaminase domain reacts with the ATP-phosphorylated UTP at the synthetase domain to give CTP. Glutamine hydrolysis is active in the presence of ATP and UTP and is stimulated by the addition of GTP. We report the crystal structures of Thermus thermophilus HB8 CTPs alone, CTPs with 3SO4(2-), and CTPs with glutamine. The enzyme is folded into a homotetramer with a cross-shaped structure. Based on the binding mode of sulfate anions to the synthetase site, ATP and UTP are computer modeled into CTPs with a geometry favorable for the reaction. Glutamine bound to the glutaminase domain is situated next to the triad of Glu-His-Cys as a catalyst and a water molecule. Structural information provides an insight into the conformational changes associated with the binding of ATP and UTP and the formation of the GTP binding site.
About this Structure
1VCM is a Protein complex structure of sequences from Thermus thermophilus. Active as CTP synthase, with EC number 6.3.4.2 Full crystallographic information is available from OCA.
Reference
Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites., Goto M, Omi R, Nakagawa N, Miyahara I, Hirotsu K, Structure. 2004 Aug;12(8):1413-23. PMID:15296735
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