Wyniki wyszukiwania dla: Subramanyam Swaminathan

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Identification of small molecule inhibitors of botulinum neurotoxin serotype E via footprint similarity

Yuchen Zhou, Brian E. McGillick, Yu-Han Gary Teng, Krupanandan Haranahalli, więcej

Bioorganic & Medicinal Chemistry > 2016 > 24 > 20 > 4875-4889

Botulinum neurotoxins (BoNT) are among the most poisonous substances known, and of the 7 serotypes (A–G) identified thus far at least 4 can cause death in humans. The goal of this work was identification of inhibitors that specifically target the light chain catalytic site of the highly pathogenic but lesser-studied E serotype (BoNT/E). Large-scale computational screening, employing the program DOCK,...

artykuł

Small molecule non-peptide inhibitors of botulinum neurotoxin serotype E: Structure–activity relationship and a pharmacophore model

Gyanendra Kumar, Rakhi Agarwal, Subramanyam Swaminathan

Bioorganic & Medicinal Chemistry > 2016 > 24 > 18 > 3978-3985

Botulinum neurotoxins (BoNTs) are the most poisonous biological substance known to humans. They cause flaccid paralysis by blocking the release of acetylcholine at the neuromuscular junction. Here, we report a number of small molecule non-peptide inhibitors of BoNT serotype E. The structure–activity relationship and a pharmacophore model are presented. Although non-peptidic in nature, these inhibitors...

artykuł

Interactions of a potent cyclic peptide inhibitor with the light chain of botulinum neurotoxin A: Insights from X-ray crystallography

Desigan Kumaran, Michael Adler, Matthew Levit, Michael Krebs, więcej

Bioorganic & Medicinal Chemistry > 2015 > 23 > 22 > 7264-7273

The seven antigenically distinct serotypes (A–G) of botulinum neurotoxin (BoNT) are responsible for the deadly disease botulism. BoNT serotype A (BoNT/A) exerts its lethal action by cleaving the SNARE protein SNAP-25, leading to inhibition of neurotransmitter release, flaccid paralysis and autonomic dysfunction. BoNTs are dichain proteins consisting of a ∼100kDa heavy chain and a ∼50kDa light chain;...

artykuł

Computer-aided identification, synthesis, and biological evaluation of novel inhibitors for botulinum neurotoxin serotype A

Yu-Han Gary Teng, William T. Berger, Natasha M. Nesbitt, Kunal Kumar, więcej

Bioorganic & Medicinal Chemistry > 2015 > 23 > 17 > 5489-5495

Botulinum neurotoxins (BoNTs) are among the most potent biological toxin known to humans, and are classified as Category A bioterrorism agents by the Centers for Disease Control and prevention (CDC). There are seven known BoNT serotypes (A–G) which have been thus far identified in literature. BoNTs have been shown to block neurotransmitter release by cleaving proteins of the soluble NSF attachment...

artykuł

2. Interaction of a novel cyclic peptide inhibitor with botulinum neurotoxin a light chain: Insights from X-ray crystallography

Michael Adler, Desigan Kumaran, Thais Moreira, Michael Krebs, więcej

Toxicon > 2015 > 93 > Supplement > S2

artykuł

185. Disassociation mechanism of progenitor complex of botulinum neurotoxin serotype E

Subramanyam Swaminathan, S. Eswaramoorthy, J. Sun, H. Li, więcej

Toxicon > 2015 > 93 > Supplement > S58

artykuł

Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5′‐phosphate

Kandavelu Palani, Stephen K. Burley, Subramanyam Swaminathan

Acta Crystallographica Section F > 69 > 1 > 15 - 19

The crystal structure of alanine racemase from Oenococcus oeni has been determined at 1.7 Å resolution using the single‐wavelength anomalous dispersion (SAD) method and selenium‐labelled protein. The protein exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites. Pyridoxal 5′‐phosphate, a cofactor, is bound to each monomer and forms a Schiff base with...

artykuł

Structure of a periplasmic glucose‐binding protein from Thermotoga maritima

Kandavelu Palani, Desigan Kumaran, Stephen K. Burley, Subramanyam Swaminathan

Acta Crystallographica Section F > 68 > 12 > 1460 - 1464

ABC transport systems have been characterized in organisms ranging from bacteria to humans. In most bacterial systems, the periplasmic component is the primary determinant of specificity of the transport complex as a whole. Here, the X‐ray crystal structure of a periplasmic glucose‐binding protein (GBP) from Thermotoga maritima determined at 2.4 Å resolution is reported. The molecule consists of two...

artykuł

Structural insight into mechanism and diverse substrate selection strategy of L‐ribulokinase

Rakhi Agarwal, Stephen K. Burley, Subramanyam Swaminathan

Proteins: Structure, Function, and Bioinformatics > 80 > 1 > 261 - 268

The araBAD operon encodes three different enzymes required for catabolism of L‐arabinose, which is one of the most abundant monosaccharides in nature. L‐ribulokinase, encoded by the araB gene, catalyzes conversion of L‐ribulose to L‐ribulose‐5‐phosphate, the second step in the catabolic pathway. Unlike other kinases, ribulokinase exhibits diversity in substrate selectivity and catalyzes phosphorylation...

artykuł

Molecular structures and functional relationships in clostridial neurotoxins

Subramanyam Swaminathan

The FEBS Journal > 278 > 23 > 4467 - 4485

The seven serotypes of Clostridium botulinum neurotoxins (A–G) are the deadliest poison known to humans. They share significant sequence homology and hence possess similar structure–function relationships. Botulinum neurotoxins (BoNT) act via a four‐step mechanism, viz., binding and internalization to neuronal cells, translocation of the catalytic domain into the cytosol and finally cleavage of one...

artykuł

Pa0148 from Pseudomonas aeruginosa Catalyzes the Deamination of Adenine

Alissa M. Goble, Zhening Zhang, J. Michael Sauder, Stephen K. Burley, więcej

Biochemistry > 2011 > 50 > 30 > 6589 - 6597

artykuł

Catalytic Mechanism and Three-Dimensional Structure of Adenine Deaminase ^,

Siddhesh S. Kamat, Ashima Bagaria, Desigan Kumaran, Gregory P. Holmes-Hampton, więcej

Biochemistry > 2011 > 50 > 11 > 1917 - 1927

artykuł

Structural basis for a ribofuranosyl binding protein: Insights into the furanose specific transport

Ashima Bagaria, Desigan Kumaran, Stephen K. Burley, Subramanyam Swaminathan

Proteins: Structure, Function, and Bioinformatics > 79 > 4 > 1352 - 1357

artykuł

Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila

Zhening Zhang, Rong Zhou, J. Michael Sauder, Peter J. Tonge, więcej

Journal of Molecular Biology > 2011 > 406 > 2 > 313-324

Fatty acyl-AMP ligase (FAAL) is a new member of a family of adenylate-forming enzymes that were recently discovered in Mycobacterium tuberculosis. They are similar in sequence to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, while FACLs perform a two-step catalytic reaction, AMP ligation followed by CoA ligation using ATP and CoA as cofactors, FAALs produce only the acyl adenylate and are...

artykuł

Structure of a putative BenF‐like porin from Pseudomonas fluorescens Pf‐5 at 2.6 Å resolution

Parthasarathy Sampathkumar, Frances Lu, Xun Zhao, Zhenzhen Li, więcej

Proteins: Structure, Function, and Bioinformatics > 78 > 14 > 3056 - 3062

artykuł

Discovery and Structure Determination of the Orphan Enzyme Isoxanthopterin Deaminase,

Richard S. Hall, Rakhi Agarwal, Daniel Hitchcock, J. Michael Sauder, więcej

Biochemistry > 2010 > 49 > 20 > 4374 - 4382

artykuł

Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein

Damodharan Lakshminarasimhan, Subramaniam Eswaramoorthy, Stephen K. Burley, Subramanyam Swaminathan

Acta Crystallographica Section F > 66 > 1 > 8 - 11

The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 Å resolution. The crystals belonged to space group P2₁, with unit‐cell parameters a = 51.85, b = 41.25, c = 55.18 Å, β = 113.4°, and contained three protein molecules in the asymmetric unit. The structure was determined by the single‐wavelength anomalous dispersion method using selenium‐labeled...

artykuł

Low pH-Induced Pore Formation by the T Domain of Botulinum Toxin Type A is Dependent upon NaCl Concentration

Bing Lai, Rakhi Agarwal, Lindsay D. Nelson, Subramanyam Swaminathan, więcej

The Journal of Membrane Biology > 2010 > 236 > 2 > 191-201

Botulinum neurotoxins (BoNTs) undergo low pH-triggered membrane insertion, resulting in the translocation of their light (catalytic) chains into the cytoplasm. The T (translocation) domain of the BoNT heavy chain is believed to carry out translocation. Here, the behavior of isolated T domain from BoNT type A has been characterized, both in solution and when associated with model membranes. When BoNT...

artykuł

Structural studies on cytosolic domain of magnesium transporter MgtE from Enterococcus faecalis

Sugadev Ragumani, J. Michael Sauder, Stephen K. Burley, Subramanyam Swaminathan

Proteins: Structure, Function, and Bioinformatics > 78 > 2 > 487 - 491

artykuł

Functional Annotation of Two New Carboxypeptidases from the Amidohydrolase Superfamily of Enzymes

Dao Feng Xiang, Chengfu Xu, Desigan Kumaran, Ann C. Brown, więcej

Biochemistry > 2009 > 48 > 21 > 4567 - 4576

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