کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5590026 | 1570078 | 2017 | 28 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
In silico characterization of TTHA0596: A potential Zn2Â + binding protein of ATP-binding cassette transporter
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کلمات کلیدی
SBPORFRMSDMSANBDAPBSPMBPATP - آدنوزین تری فسفات یا ATPIron - آهنmultiple sequence alignment - ترتیب توالی چندگانهnucleotide binding domain - دامنه اتصال نوکلئوتیدیopen reading frame - قاب خواندن بازManganese - منگنز root mean square deviation - میانگین انحراف مربع ریشهHypothetical protein - پروتئین هیپوتیتیATP-binding cassette - کیت اتصال به ATP
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
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چکیده انگلیسی
Metalloproteins, the most diverse classes of proteins, require metal ions (Mn2Â +, Zn2Â +, Ni2Â +, Fe2Â +/3Â +, etc.) for their regulatory, catalytic and/or structural activities making them inevitable for survival of an organism. One of the most efficient systems of acquiring metal ions inside a bacterial cell is the ATP-binding cassette (ABC) transporters, which are further classified into importers and exporters. Structurally, ABC importers comprises of a transmembrane domain, a nucleotide binding domain and a substrate binding protein (SBP) for substrate acquisition. Being specific to prokaryotes and often accountable for their pathogenicity, SBPs are recognized as potential drug targets. In this study, TTHA0596, a SBP from Thermus thermophilus HB8 is characterized using in silico approaches. Homology search and phylogenetic tree analysis exhibit that TTHA0596 is similar to a group of Zn2Â +/Mn2Â + binding SBPs. Furthermore, TTHA0596 protein attains an unusual structural prototype similar to that of cluster A-I SBPs. Akin to Zn2Â + binding SBPs, binding pocket of TTHA0596 is constituted of three histidine residues (His52, His123 and His185). However, the presence of an aspartate (Asp259) and absence of the histidine-rich loop, an attribute of Zn2Â + binding SBPs, indicates its possible affinity towards Mn2Â + ion. This further led us to identify a subdivision within the Zn2Â + binding SBPs, (Altschul et al., 1990) group I display affinity for both Zn2Â + and Mn2Â + ions, while (Ammendola et al., 2007) group II are highly specific towards Zn2Â + ion. Our analysis concludes that TTHA0596 protein belongs to group I Zn2Â + binding SBPs and thus bear a tendency to bind both Zn2Â + and Mn2Â + ions.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene Reports - Volume 6, March 2017, Pages 132-141
Journal: Gene Reports - Volume 6, March 2017, Pages 132-141
نویسندگان
Suraj Kumar Mandal, Monika Chandravanshi, Prerana Gogoi, Shankar Prasad Kanaujia,