Zobrazeno 1 - 10
of 25
pro vyhledávání: '"David T. Gallagher"'
Autor:
Javier Gutiérrez-Fernández, Karol Kaszuba, Gurdeep S. Minhas, Rozbeh Baradaran, Margherita Tambalo, David T. Gallagher, Leonid A. Sazanov
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
Complex I (NADH:ubiquinone oxidoreductase) is the first enzyme of the respiratory chain in bacteria and mitochondria. Here, the authors present cryo-EM and crystal structures of T. thermophilus complex I in different conformational states and further
Externí odkaz:
https://doaj.org/article/2865989836bc44c684807dba957f46af
Autor:
J. Gutierrez-Fernandez, Karol Kaszuba, David T. Gallagher, Rozbeh Baradaran, G.S. Minhas, Margherita Tambalo, Leonid A. Sazanov
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
'Nature Communications ', vol: 11, pages: 4135-1-4135-17 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
'Nature Communications ', vol: 11, pages: 4135-1-4135-17 (2020)
Complex I is the first and the largest enzyme of respiratory chains in bacteria and mitochondria. The mechanism which couples spatially separated transfer of electrons to proton translocation in complex I is not known. Here we report five crystal str
Publikováno v:
Data in Brief
Data in Brief, Vol 16, Iss, Pp 29-36 (2018)
Data in Brief, Vol 16, Iss, Pp 29-36 (2018)
The reported data describe the crystallization, crystal packing, structure determination and twinning of the unliganded Fab (antigen-binding fragment) from the NISTmAb (standard reference material 8671). The raw atomic coordinates are available as Pr
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 74(Pt 9)
As the link between antigen binding and immune activation, the antibody Fc region has received extensive structural study. In this report, the structure of the Fc fragment of the NIST IgG1 mAb (reference material 8671) is described at 2.1 Å resoluti
Publikováno v:
Journal of Molecular Biology. 405:787-803
Adenylyl cyclases (ACs) belonging to three nonhomologous classes (II, III, and IV) have been structurally characterized, enabling a comparison of the mechanisms of cyclic adenosine 3',5'-monophosphate biosynthesis. We report the crystal structures of
Autor:
David T. Gallagher, Karol Kaszuba, Margherita Tambalo, J. Gutierrez-Fernandez, Leonid A. Sazanov
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859:e40
Autor:
Martin P. Mayhew, Andrew Howard, David T. Gallagher, Salita Kaistha, Natasha Smith, Adrian E. Roitberg, Eva Rivera, Marcia J. Holden
Publikováno v:
Archives of Biochemistry and Biophysics. 445:72-80
Chorismate lyase (CL) removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. We previously reported the crystal structure at 1.4 A resolution of the Escherichia coli CL with bound 4HB product, showing
Autor:
David T. Gallagher, Harold G. Monbouquette, Imke Schröder, Hugh Robinson, Natasha Smith, Marcia J. Holden
Publikováno v:
Journal of Molecular Biology. 342:119-130
The hyperthermophilic archaeon Archaeoglobus fulgidus contains an l-Ala dehydrogenase (AlaDH, EC 1.4.1.1) that is not homologous to known bacterial dehydrogenases and appears to represent a previously unrecognized archaeal group of NAD-dependent dehy
Autor:
David T. Gallagher, Martin P. Mayhew, Annie Heroux, Natasha Smith, David Charlton, Marcia J. Holden, Howard Robinson
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:2328-2331
Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon Archaeoglobus fulgidus is a dimer of 35 kDa chains. The archaeal enzyme appears to represent a new class of AlaDH that is not homologous to bacterial AlaDH enzymes, but has close evolu
Autor:
Patrick Alexander, David T. Gallagher, Jane E. Ladner, Orna Almog, Philip N. Bryan, Gary L. Gilliland, Susan L. Strausberg
Publikováno v:
Journal of Biological Chemistry. 277:27553-27558
The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 A resolution, respectively. The micromolar affinity calcium binding site (site A) has been deleted (Delta75-83) in these varian