1vcm

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[[Image:1vcm.gif|left|200px]]<br /><applet load="1vcm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vcm.gif|left|200px]]
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caption="1vcm, resolution 2.35&Aring;" />
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'''Crystal Structure of T.th. HB8 CTP synthetase'''<br />
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{{Structure
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|PDB= 1vcm |SIZE=350|CAPTION= <scene name='initialview01'>1vcm</scene>, resolution 2.35&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE= HB8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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}}
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'''Crystal Structure of T.th. HB8 CTP synthetase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1VCM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCM OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15296735 15296735]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15296735 15296735]
[[Category: CTP synthase]]
[[Category: CTP synthase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: tetramer]]
[[Category: tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:43:45 2008''

Revision as of 12:43, 20 March 2008


PDB ID 1vcm

Drag the structure with the mouse to rotate
, resolution 2.35Å
Gene: HB8 (Thermus thermophilus)
Activity: CTP synthase, with EC number 6.3.4.2
Coordinates: save as pdb, mmCIF, xml



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. 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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