Structure of a short-chain dehydrogenase/reductase (SDR) within a genomic island from a clinical strain ofAcinetobacter baumannii
| العنوان: | Structure of a short-chain dehydrogenase/reductase (SDR) within a genomic island from a clinical strain ofAcinetobacter baumannii |
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| المؤلفون: | Stephen J. Harrop, Ian T. Paulsen, Bridget C. Mabbutt, Bhumika S. Shah, Sasha G. Tetu |
| المصدر: | Acta Crystallographica. Section F, Structural Biology Communications |
| بيانات النشر: | International Union of Crystallography (IUCr), 2014. |
| سنة النشر: | 2014 |
| مصطلحات موضوعية: | Acinetobacter baumannii, Models, Molecular, Rossmann fold, Acinetobacter baumannii WM99c, Genomic Islands, Molecular Sequence Data, Biophysics, Dehydrogenase, Reductase, Crystallography, X-Ray, Biochemistry, Apoenzymes, Bacterial Proteins, multidrug resistance, Structural Biology, Catalytic Domain, Genomic island, Genetics, Structural Communications, NADH, NADPH Oxidoreductases, Amino Acid Sequence, Peptide sequence, Short-chain dehydrogenase, biology, opportunistic pathogen, Active site, Condensed Matter Physics, biology.organism_classification, biology.protein, Fatty Acid Synthases, Genome, Bacterial, nosocomial strain |
| الوصف: | The structure of a short-chain dehydrogenase encoded within genomic islands of A. baumannii strains has been solved to 2.4 Å resolution. This classical SDR incorporates a flexible helical subdomain. The NADP-binding site and catalytic side chains are identified. Over 15% of the genome of an Australian clinical isolate of Acinetobacter baumannii occurs within genomic islands. An uncharacterized protein encoded within one island feature common to this and other International Clone II strains has been studied by X-ray crystallography. The 2.4 Å resolution structure of SDR-WM99c reveals it to be a new member of the classical short-chain dehydrogenase/reductase (SDR) superfamily. The enzyme contains a nucleotide-binding domain and, like many other SDRs, is tetrameric in form. The active site contains a catalytic tetrad (Asn117, Ser146, Tyr159 and Lys163) and water molecules occupying the presumed NADP cofactor-binding pocket. An adjacent cleft is capped by a relatively mobile helical subdomain, which is well positioned to control substrate access. |
| تدمد: | 2053-230X |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ef1d1daf04730f7e777b20e685adfc3 https://doi.org/10.1107/s2053230x14019785 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....8ef1d1daf04730f7e777b20e685adfc3 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 2053230X |
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