Search Results - "Kuranova, Inna P"

The nature of the ligand's side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex by Akparov, Valery Kh, Timofeev, Vladimir I, Konstantinova, Galina E, Khaliullin, Ilyas G, Kuranova, Inna P, Rakitina, Tatiana V, Švedas, Vytas

“…The carboxypeptidase T (CPT) from Thermoactinomyces vulgaris has an active site structure and 3D organization similar to pancreatic carboxypeptidases A and B…”
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Crystal Structure of Inhibitor-Bound Bacterial Oligopeptidase B in the Closed State: Similarity and Difference between Protozoan and Bacterial Enzymes by Petrenko, Dmitry E, Karlinsky, David M, Gordeeva, Veronika D, Arapidi, Georgij P, Britikova, Elena V, Britikov, Vladimir V, Nikolaeva, Alena Y, Boyko, Konstantin M, Timofeev, Vladimir I, Kuranova, Inna P, Mikhailova, Anna G, Bocharov, Eduard V, Rakitina, Tatiana V

“…The crystal structure of bacterial oligopeptidase B from (SpOpB) in complex with a chloromethyl ketone inhibitor was determined at 2.2 Å resolution. SpOpB was…”
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First Crystal Structure of Bacterial Oligopeptidase B in an Intermediate State: The Roles of the Hinge Region Modification and Spermine by Petrenko, Dmitry E., Timofeev, Vladimir I., Britikov, Vladimir V., Britikova, Elena V., Kleymenov, Sergey Y., Vlaskina, Anna V., Kuranova, Inna P., Mikhailova, Anna G., Rakitina, Tatiana V.

“…Oligopeptidase B (OpB) is a two-domain, trypsin-like serine peptidase belonging to the S9 prolyloligopeptidase (POP) family. Two domains are linked by a hinge…”
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The Crystal Structure of Nα-p-tosyl-lysyl Chloromethylketone-Bound Oligopeptidase B from Serratia Proteamaculans Revealed a New Type of Inhibitor Binding by Timofeev, Vladimir, Petrenko, Dmitry, Agapova, Yulia, Vlaskina, Anna, Karlinsky, David, Mikhailova, Anna, Kuranova, Inna, Rakitina, Tatiana

“…A covalent serine protease inhibitor—Na-p-Tosyl-Lysyl Chloromethylketone (TCK) is a modified lysine residue tosylated at the N-terminus and chloromethylated at…”
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Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine by Akparov, Valery Kh, Konstantinova, Galina E., Timofeev, Vladimir I., Khaliullin, Ilyas G., Kuranova, Inna P.

“…Carboxypeptidase T (CPT) from Thermoactinomyces vulgaris (EC 3.4.17.18) has a broad substrate specificity, the mechanism of which remains unclear. It cleaves…”
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The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27 by Timofeev, Vladimir I., Fateev, Ilya V., Kostromina, Maria A., Abramchik, Yuliya A., Konstantinova, Irina D., Volkov, Vladimir V., Lykoshin, Dmitry D., Mikheeva, Olga O., Muravieva, Tatiana I., Esipov, Roman S., Kuranova, Inna P.

“…Two recombinant purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27 encoded by genes TT_C1070 (TthPNPI) and TT_C0194…”
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The binding of precipitant ions in the tetragonal crystals of hen egg white lysozyme by Marchenkova, Margarita A., Kuranova, Inna P., Timofeev, Vladimir I., Boikova, Anastasiia S., Dorovatovskii, Pavel V., Dyakova, Yulia A., Ilina, Kseniia B., Pisarevskiy, Yury V., Kovalchuk, Mikhail V.

“…The bonds between lysozyme molecules and precipitant ions in single crystals grown with chlorides of several metals are analysed on the basis of crystal…”
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Structural insights into the broad substrate specificity of carboxypeptidase T from Thermoactinomyces vulgaris by Akparov, Valery Kh, Timofeev, Vladimir I, Khaliullin, Ilyas G, Švedas, Vytas, Chestukhina, Galina G, Kuranova, Inna P

“…The crystal structures of carboxypeptidase T (CpT) complexes with phenylalanine and arginine substrate analogs – benzylsuccinic acid and…”
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Crystal structures of carboxypeptidase T complexes with transition-state analogs by Akparov, Valery Kh, Timofeev, Vladimir I., Khaliullin, Ilyas G., Švedas, Vytas, Kuranova, Inna P., Rakitina, Tatiana V.

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Crystal structure of mutant carboxypeptidase T from Thermoactinomyces vulgaris with an implanted S1′ subsite from pancreatic carboxypeptidase B by Akparov, Valery Kh, Timofeev, Vladimir I., Kuranova, Inna P., Rakitina, Tatiana V.

“…A site‐directed mutagenesis method has been used to obtain the G215S/A251G/T257A/D260G/T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris…”
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Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir by Timofeev, Vladimir I., Zhukhlistova, Nadezhda E., Abramchik, Yuliya A., Muravieva, Tatiana I., Esipov, Roman S., Kuranova, Inna P.

“…Escherichia coli purine nucleoside phosphorylase (PNP), which catalyzes the reversible phosphorolysis of purine ribonucleosides, belongs to the family I…”
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Crystal Structure of the Protealysin Precursor: INSIGHTS INTO PROPEPTIDE FUNCTION by Demidyuk, Ilya V, Gromova, Tania Yu, Polyakov, Konstantin M, Melik-Adamyan, William R, Kuranova, Inna P, Kostrov, Sergey V

“…Protealysin (PLN) belongs to the M4 family of peptidases that are commonly known as thermolysin-like proteases (TLPs). All TLPs are synthesized as precursors…”
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Crystal structure of Escherichia coli purine nucleoside phosphorylase in complex with 7‐deazahypoxanthine by Timofeev, Vladimir I., Zhukhlistova, Nadezhda E., Abramchik, Yuliya A., Fateev, Ilya I., Kostromina, Maria A., Muravieva, Tatiana I., Esipov, Roman S., Kuranova, Inna P.

“…Purine nucleoside phosphorylases (EC 2.4.2.1; PNPs) reversibly catalyze the phosphorolytic cleavage of glycosidic bonds in purine nucleosides to generate…”
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Crystal structure of recombinant phosphoribosylpyrophosphate synthetase 2 from Thermus thermophilus HB27 complexed with ADP and sulfate ions by Timofeev, Vladimir I., Sinitsyna, Ekaterina V., Kostromina, Maria A., Muravieva, Tatiana I., Makarov, Dmitry A., Mikheeva, Olga O., Kuranova, Inna P., Esipov, Roman S.

“…Phosphoribosylpyrophosphate synthetase (PRPPS) from the thermophilic bacterial strain Thermus thermophilus HB27 catalyzes the synthesis of…”
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Processing of protealysin precursor by Gromova, Tania Yu, Demidyuk, Ilya V., Kozlovskiy, Viacheslav I., Kuranova, Inna P., Kostrov, Sergey V.

“…Protealysin, a protease previously described by us in Serratia proteamaculans, belongs to the group of thermolysin-like proteases (TLPs) that differ from…”
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Crystallization and preliminary X-ray diffraction studies of the family 54 carbohydrate-binding module from laminarinase (β-1,3-glucanase) Lic16A of Clostridium thermocellum by Kislitsyn, Yury A., Samygina, Valeriya R., Dvortsov, Igor A., Lunina, Nataliya A., Kuranova, Inna P., Velikodvorskaya, Galina A.

“…The crystallization and preliminary X‐ray diffraction analysis of the carbohydrate‐binding module (CBM) from laminarinase Lic16A of the hyperthermophilic…”
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Crystal Structure of the Protealysin Precursor by Demidyuk, Ilya V., Gromova, Tania Yu, Polyakov, Konstantin M., Melik-Adamyan, William R., Kuranova, Inna P., Kostrov, Sergey V.

“…Protealysin (PLN) belongs to the M4 family of peptidases that are commonly known as thermolysin-like proteases (TLPs). All TLPs are synthesized as precursors…”
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The Crystal Structure of Glutamyl Endopeptidase from Bacillus intermedius Reveals a Structural Link between Zymogen Activation and Charge Compensation by Meijers, Rob, Blagova, Elena V, Levdikov, Vladimir M, Rudenskaya, Galina N, Chestukhina, Galina G, Akimkina, Tatiana V, Kostrov, Sergei V, Lamzin, Victor S, Kuranova, Inna P

“…Extracellular glutamyl endopeptidase from Bacillus intermedius (BIEP) is a chymotrypsin-like serine protease which cleaves the peptide bond on the carboxyl…”
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X-ray structure of recombinant house dust mite allergen Der p 3 by Timofeev, Vladimir I., Abramchik, Yulia A., Shevtsov, Mikhail B., Kostromina, Maria A., Zavriev, Sergey K., Zayats, Evgeny A., Esipov, Roman S., Kuranova, Inna P.

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X‐Ray Structure of Yeast Inorganic Pyrophosphatase Complexed with Manganese and Phosphate by Harutyunyan, Emil H., Kuranova, Inna P., Vainshtein, Boris K., Höhne, Wolfgang E., Lamzin, Victor S., Dauter, Zbigniew, Teplyakov, Alexei V., Wilson, Keith S.

“…The three‐dimensional structure of the manganese‐phosphate complex of inorganic pyrophosphatase from Saccharomyces cerevisiae has been refined to an R factor…”
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