00607nas a2200181   4500008004100000022001400041245007300055210006900128260000800197300000900205490000700214653001400221653002400235653001800259100001900277700002600296856010300322       2014                        eng d  a2053-273300aAllostery mapping in enterococcus faecalis Bile Salt Hydrolase (BSH)0 aAllostery mapping in enterococcus faecalis Bile Salt Hydrolase B  cMAY  aC2740 v7010aAllostery10aBile salt hydrolase10aMD Simulation1 aYadav, Yashpal1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/allostery-mapping-enterococcus-faecalis-bile-salt-hydrolase-bsh01872nas a2200157   4500008004100000245009900041210006900140260000800209300001200217490000800229520128800237100002201525700002601547700001901573856012201592       2018                        eng d00aAnalysis of Kunitz inhibitors from plants for comprehensive structural and functional insights0 aAnalysis of Kunitz inhibitors from plants for comprehensive stru  cJUL  a933-9430 v1133 aLegume Kunitz type trypsin inhibitor (KTI) family is one of the most versatile families of proteins. A typical KTI features a single peptide folded in beta-trefoil manner, with the molecular weight about 20-22 kDa and two disulphide bonds. The members are known to inhibit a wide range of serpins proteases at the same time many of them possess unique features. Copaifera langsdoiffii Trypsin inhibitor (CTI) has a beta-trefoil fold made up of two non-covalently bound polypeptide chains with only a single disulfide bridge. Delonix regia Trypsin inhibitor (DrTI) has one amino acid insertion between P1 and P2 of the reactive site distorting its conformation. Bauhinia bauhinioides Cruzipain inhibitor (BbCI) has a conservative beta-trefoil fold but lacks disulfide bonds. Such subtle differences in structures make Kunitz inhibitors different from other inhibitor families. Most of the studies on these inhibitors are focused towards their proposed role in defense from insect pests and wounding but their exact physiological role in nature is still uncharted. Thus, it would be very interesting to closely analyze the structural details of these inhibitors in order to ascertain their biological role and other fascinating applications. (C) 2018 Elsevier B.V. All rights reserved.1 aBendre, Ameya, D.1 aRamasamy, Sureshkumar1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/analysis-kunitz-inhibitors-plants-comprehensive-structural-and-functional-insights02238nas a2200169   4500008004100000245007000041210006900111260000800180300001200188490000700200520167100207100001701878700002101895700002701916700002601943856009901969       2018                        eng d00aAnalysis of tail-anchored protein translocation pathway in plants0 aAnalysis of tailanchored protein translocation pathway in plants  cJUL  a161-1670 v143 aTail-anchored (TA) proteins are a special class of membrane proteins that carry out vital functions in all living cells. Targeting mechanisms of TA proteins are investigated as the best example for post-translational protein targeting in yeast. Of the several mechanisms, Guided Entry of Tail-anchored protein (GET) pathway plays a major role in TA protein targeting. Many in silico and in vivo analyses are geared to identify TA proteins and their targeting mechanisms in different systems including Arabidopsis thaliana. Yet, crop plants that grow in specific and/or different conditions are not investigated for the presence of TA proteins and GET pathway. This study majorly investigates GET pathway in two crop plants, Oryza sativa subsp. Indica and Solanum tuberosum, through detailed in silico analysis. 508 and 912 TA proteins are identified in Oryza sativa subsp. Indica and Solanum tuberosum respectively and their localization with respect to endoplasmic reticulum (ER), mitochondria, and chloroplast has been delineated. Similarly, the associated GET proteins are identified (Get1, Get3 and Get4) and their structural inferences are elucidated using homology modelling. Get3 models are based on yeast Get3. The cytoplasmic Get3 from O. sativa is identified to be very similar to yeast Get3 with conserved P-loop and TA binding groove. Three cytoplasmic Get3s are identified for S. tuberosum. Taken together, this is the first study to identify TA proteins and GET components in Oryza sativa subsp. Indica and Solanum tuberosum, forming the basis for any further experimental characterization of TA targeting and GET pathway mechanisms in crop plants.

1 aManu, M., S.1 aGhosh, Deepanjan1 aChaudhari, Bhushan, P.1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/analysis-tail-anchored-protein-translocation-pathway-plants02373nas a2200241   4500008004100000022001400041245013900055210006900194260000800263300001200271490000700283520152500290653001901815653002001834653001101854653002101865653002001886653002101906100002001927700003001947700002601977856012802003       2020                        eng d  a0929-866500aArcheal Di-O-geranylgeranyl glyceryl phosphate synthase of a UbiA superfamily member provides insight into the multiple human diseases0 aArcheal DiOgeranylgeranyl glyceryl phosphate synthase of a UbiA   cJAN  a568-5730 v273 a<p>One of the unique characteristic features of the domain archaea, are the lipids that form the hydrophobic core of their cell membrane. These membrane lipids are characterized by distinctive isoprenoid biochemistry and the building blocks are two core lipid structures, sn-2,3-diphytanyl glycerol diether (archaeol) and sn-2,3-dibiphytanyl diglycerol tetraether (caldarchaeol). Archaeol has two phytanyl chains (C-20 in a bilayer structure connected to the glycerol moiety by an ether bond. The enzyme involved in this bilayer formation is Di-O-Geranylgeranyl Glyceryl Phosphate Synthase (DGGGPS), which is a member of a very versatile superfamily of enzymes known as UbiA superfamily. Multiple sequence analysis of the typical members of the UbiA superfamily indicates that the majority of conserved residues are located around the central cavity of these enzymes. Interestingly few of these conserved residues in the human homologs are centrally implicated in several human diseases, on basis of the major mutations reported against these diseases in the earlier clinical studies. It remains to he investigated about the role of these conserved residues in the biochemistiy of these enzymes. The binding and active site of these enzymes found to be similar architecture but have different substrate affinities ranging from aromatic to linear compounds. So further investigation of UbiA superfamily may be translated to novel therapeutic and diagnostic application of these proteins in human disease management.</p>
10aArcheal lipids10abiA superfamily10aDGGGPS10agenetic diseases10alipid synthesis10amembrane protein1 aBoral, Debjyoti1 aRao, Vamkudoth, Koteswara1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/archeal-di-o-geranylgeranyl-glyceryl-phosphate-synthase-ubia-superfamily-member-provides