کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5591496 | 1404978 | 2017 | 39 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural and functional characterization of a cold adapted TPM-domain with ATPase/ADPase activity
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کلمات کلیدی
β,γ-methyleneadenosine 5′-triphosphatepSerSLSO-Phospho-L-SerineNTPDaseAMP-PCPLCRNTPDasesDLSpNPPp-nitrophenylphosphate - p-نیترفنیل فسفاتCold-adaptation - انطباق سردX-ray crystallography - بلورنگاری پرتو-ایکسcircular dichroism - رنگ تابی دورانیPsychrophiles - روانشناسیATPase activity - فعالیت ATPasenucleoside triphosphate diphosphohydrolase - نوکلئوزید تری فسفات دی فسفو هیدرولازstatic light scattering - پراکندگی نور استاتیکDynamic Light Scattering - پراکندگی نور دینامیکی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Structural and functional characterization of a cold adapted TPM-domain with ATPase/ADPase activity Structural and functional characterization of a cold adapted TPM-domain with ATPase/ADPase activity](/preview/png/5591496.png)
چکیده انگلیسی
The Pfam PF04536 TPM_phosphatase family is a broadly conserved family of domains found across prokaryotes, plants and invertebrates. Despite having a similar protein fold, members of this family have been implicated in diverse cellular processes and found in varied subcellular localizations. Very recently, the biochemical characterization of two evolutionary divergent TPM domains has shown that they are able to hydrolyze phosphate groups from different substrates. However, there are still incorrect functional annotations and uncertain relationships between the structure and function of this family of domains. BA41 is an uncharacterized single-pass transmembrane protein from the Antarctic psychrotolerant bacterium Bizionia argentinensis with a predicted compact extracytoplasmic TPM domain and a C-terminal cytoplasmic low complexity region. To shed light on the structural properties that enable TPM domains to adopt divergent roles, we here accomplish a comprehensive structural and functional characterization of the central TPM domain of BA41 (BA41-TPM). Contrary to its predicted function as a beta-propeller methanol dehydrogenase, light scattering and crystallographic studies showed that BA41-TPM behaves as a globular monomeric protein and adopts a conserved Rossmann fold, typically observed in other TPM domain structures. Although the crystal structure reveals the conservation of residues involved in substrate binding, no putative catalytic or intramolecular metal ions were detected. Most important, however, extensive biochemical studies demonstrated that BA41-TPM has hydrolase activity against ADP, ATP, and other di- and triphosphate nucleotides and shares properties of cold-adapted enzymes. The role of BA41 in extracellular ATP-mediated signaling pathways and its occurrence in environmental and pathogenic microorganisms is discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 197, Issue 3, March 2017, Pages 201-209
Journal: Journal of Structural Biology - Volume 197, Issue 3, March 2017, Pages 201-209
نویسندگان
MarÃa L. Cerutti, Lisandro H. Otero, Clara Smal, Leonardo Pellizza, Fernando A. Goldbaum, Sebastián Klinke, MartÃn Aran,