1wkq
From Proteopedia
(New page: 200px<br /><applet load="1wkq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wkq, resolution 1.17Å" /> '''Crystal Structure of...) |
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| - | [[Image:1wkq.gif|left|200px]]<br /><applet load="1wkq" size=" | + | [[Image:1wkq.gif|left|200px]]<br /><applet load="1wkq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wkq, resolution 1.17Å" /> | caption="1wkq, resolution 1.17Å" /> | ||
'''Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped structure in the cytidine deaminase superfamily'''<br /> | '''Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped structure in the cytidine deaminase superfamily'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Guanine deaminase, a key enzyme in the nucleotide metabolism, catalyzes | + | Guanine deaminase, a key enzyme in the nucleotide metabolism, catalyzes the hydrolytic deamination of guanine into xanthine. The crystal structure of the 156-residue guanine deaminase from Bacillus subtilis has been solved at 1.17-A resolution. Unexpectedly, the C-terminal segment is swapped to form an intersubunit active site and an intertwined dimer with an extensive interface of 3900 A(2) per monomer. The essential zinc ion is ligated by a water molecule together with His(53), Cys(83), and Cys(86). A transition state analog was modeled into the active site cavity based on the tightly bound imidazole and water molecules, allowing identification of the conserved deamination mechanism and specific substrate recognition by Asp(114) and Tyr(156'). The closed conformation also reveals that substrate binding seals the active site entrance, which is controlled by the C-terminal tail. Therefore, the domain swapping has not only facilitated the dimerization but has also ensured specific substrate recognition. Finally, a detailed structural comparison of the cytidine deaminase superfamily illustrates the functional versatility of the divergent active sites found in the guanine, cytosine, and cytidine deaminases and suggests putative specific substrate-interacting residues for other members such as dCMP deaminases. |
==About this Structure== | ==About this Structure== | ||
| - | 1WKQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Guanine_deaminase Guanine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.3 3.5.4.3] Full crystallographic information is available from [http:// | + | 1WKQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Guanine_deaminase Guanine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.3 3.5.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Guanine deaminase]] | [[Category: Guanine deaminase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chang, Y | + | [[Category: Chang, Y J.]] |
| - | [[Category: Lai, C | + | [[Category: Lai, C T.]] |
| - | [[Category: Liaw, S | + | [[Category: Liaw, S H.]] |
[[Category: IMD]] | [[Category: IMD]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: the cytidine deaminase superfamily]] | [[Category: the cytidine deaminase superfamily]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:23 2008'' |
Revision as of 13:45, 21 February 2008
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Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped structure in the cytidine deaminase superfamily
Overview
Guanine deaminase, a key enzyme in the nucleotide metabolism, catalyzes the hydrolytic deamination of guanine into xanthine. The crystal structure of the 156-residue guanine deaminase from Bacillus subtilis has been solved at 1.17-A resolution. Unexpectedly, the C-terminal segment is swapped to form an intersubunit active site and an intertwined dimer with an extensive interface of 3900 A(2) per monomer. The essential zinc ion is ligated by a water molecule together with His(53), Cys(83), and Cys(86). A transition state analog was modeled into the active site cavity based on the tightly bound imidazole and water molecules, allowing identification of the conserved deamination mechanism and specific substrate recognition by Asp(114) and Tyr(156'). The closed conformation also reveals that substrate binding seals the active site entrance, which is controlled by the C-terminal tail. Therefore, the domain swapping has not only facilitated the dimerization but has also ensured specific substrate recognition. Finally, a detailed structural comparison of the cytidine deaminase superfamily illustrates the functional versatility of the divergent active sites found in the guanine, cytosine, and cytidine deaminases and suggests putative specific substrate-interacting residues for other members such as dCMP deaminases.
About this Structure
1WKQ is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Guanine deaminase, with EC number 3.5.4.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus subtilis guanine deaminase: the first domain-swapped structure in the cytidine deaminase superfamily., Liaw SH, Chang YJ, Lai CT, Chang HC, Chang GG, J Biol Chem. 2004 Aug 20;279(34):35479-85. Epub 2004 Jun 4. PMID:15180998
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