Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Geeta Kapadia"'
Autor:
Andrew Howard, Alan Peterkofsky, Kap Lim, Alexey Teplyakov, Celia C. H. Chen, Jennifer Schwartz, Osnat Herzberg, Prasad T. Reddy, Peng Peng Zhu, Geeta Kapadia
Publikováno v:
Proceedings of the National Academy of Sciences. 103:16218-16223
Bacterial transport of many sugars, coupled to their phosphorylation, is carried out by the phosphoenolpyruvate (PEP):sugar phosphotransferase system and involves five phosphoryl group transfer reactions. Sugar translocation initiates with the Mg 2+
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61c233e8f16358dd7cbaa0288fcf2960
https://doi.org/10.1073/pnas.0607587103
https://doi.org/10.1073/pnas.0607587103
Publikováno v:
Structure. 6:75-88
Background: The proteins of halophilic archaea require high salt concentrations both for stability and for activity, whereas they denature at low ionic strength. The structural basis for this phenomenon is not yet well understood. The crystal structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20d34146a8fd3c85108a7fa29236e0e0
https://doi.org/10.1016/s0969-2126(98)00009-4
https://doi.org/10.1016/s0969-2126(98)00009-4
Autor:
Celia C. H. Chen, Lawrence J. Carroll, Geeta Kapadia, Osnat Herzberg, Seong J. Noh, Marielena McGuire, Debra Dunaway-Mariano
Publikováno v:
Proceedings of the National Academy of Sciences. 93:2652-2657
The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals a three-domain molecule in which the phosphohistidine domain is flanked by the nucleotide and the phosphoeno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cd4e02e413324293b9c1933d9504a28
https://doi.org/10.1073/pnas.93.7.2652
https://doi.org/10.1073/pnas.93.7.2652
Autor:
Geeta Kapadia, Osnat Herzberg, John Moult, Celia C. H. Chen, Zhong Li, Laura E. Zawadzke, Susana Wäsch, Soojay Banerjee
Publikováno v:
Biochemistry. 35:16475-16482
Two site-directed mutant enzymes of the class A beta-lactamase from Staphylococcus aureus PC1 were produced with the goal of blocking the site that in the native enzyme is occupied by the proposed hydrolytic water molecule. The crystal structures of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74aa2e088a709bc3d646fa66d6fc6432
https://doi.org/10.1021/bi962242a
https://doi.org/10.1021/bi962242a
Publikováno v:
Proceedings of the National Academy of Sciences. 91:1428-1432
The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers assoc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31c2d3bf2b9c97a6f30ddc222fca1611
https://doi.org/10.1073/pnas.91.4.1428
https://doi.org/10.1073/pnas.91.4.1428
Autor:
S. L. Sutrina, Osnat Herzberg, Jonathan Reizer, Milton H. Saier, Prasad T. Reddy, Geeta Kapadia
Publikováno v:
Proceedings of the National Academy of Sciences. 89:2499-2503
The crystal structure of the histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.0-A resolution and refined to a crystallographic residual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9278e431c6af80fd9bdf0b0b06b21427
https://doi.org/10.1073/pnas.89.6.2499
https://doi.org/10.1073/pnas.89.6.2499
Autor:
Geeta Kapadia, Milton H. Saier, Jonathan Reizer, Der Ing Liao, Prasad T. Reddy, Osnat Herzberg
Publikováno v:
Biochemistry. 30:9583-9594
The crystal structure of the IIA domain of the glucose permease of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.2-A resolution. Refinement of the structure is in progress, and the curre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74e2db4ef9375dc010416fc556350d70
https://doi.org/10.1021/bi00104a004
https://doi.org/10.1021/bi00104a004
Publikováno v:
Biochemistry. 37(10)
The structure of class A beta-lactamases contains an omega-loop associated with the active site, which carries a key catalytic residue, Glu166. A 16-residue omega-loop deletion mutant of beta-lactamase from Staphylococcus aureus PC1, encompassing res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42851a1333e23ec759aa17a5e0293c0e
https://pubmed.ncbi.nlm.nih.gov/9521648
https://pubmed.ncbi.nlm.nih.gov/9521648
Autor:
Thomas J. Smith, and Andrew Coulson, Geeta Kapadia, Celia C. Chen, Laura E. Zawadzke, Osnat Herzberg, Susana Wäsch
Publikováno v:
Biochemistry. 35(38)
Two mutant beta-lactamases from Staphylococcus aureus PC1 which probe key catalytic residues have been produced by site-directed mutagenesis. In the S70A enzyme, the nucleophilic group that attacks the beta-lactam carbonyl carbon atom was eliminated.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42ba8b627515f99fe1e5e087faafbb18
https://pubmed.ncbi.nlm.nih.gov/8823158
https://pubmed.ncbi.nlm.nih.gov/8823158
Publikováno v:
Biochemistry. 30(39)
The crystal structure of a mutant protein of a class A beta-lactamase from Staphylococcus aureus PC1, in which Asp179 is replaced by an asparagine (P54), has been determined and refined at 2.3-A resolution (1 A = 0.1 nm). The resulting crystallograph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d977b0861e0fe53337f6d75e575a3ca0
https://pubmed.ncbi.nlm.nih.gov/1892849
https://pubmed.ncbi.nlm.nih.gov/1892849