1wkq

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{{STRUCTURE_1wkq| PDB=1wkq | SCENE= }}
{{STRUCTURE_1wkq| PDB=1wkq | SCENE= }}
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'''Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped structure in the cytidine deaminase superfamily'''
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===Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped structure in the cytidine deaminase superfamily===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15180998}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15180998 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15180998}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15180998 15180998]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15180998 15180998]
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Crystallization and preliminary crystallographic analysis of Bacillus subtilis guanine deaminase., Chang YJ, Huang CH, Hu CY, Liaw SH, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1152-4. Epub 2004, May 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15159585 15159585]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Guanine deaminase]]
[[Category: Guanine deaminase]]
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[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
[[Category: The cytidine deaminase superfamily]]
[[Category: The cytidine deaminase superfamily]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:48:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:37:33 2008''

Revision as of 13:37, 27 July 2008

Template:STRUCTURE 1wkq

Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped structure in the cytidine deaminase superfamily

Template:ABSTRACT PUBMED 15180998

About this Structure

1WKQ is a Single protein structure of sequence from Bacillus subtilis. 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

Crystallization and preliminary crystallographic analysis of Bacillus subtilis guanine deaminase., Chang YJ, Huang CH, Hu CY, Liaw SH, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1152-4. Epub 2004, May 21. PMID:15159585

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