Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Katherine A, Pattridge"'
Publikováno v:
Proceedings of the National Academy of Sciences. 106:18527-18532
Cobalamin-dependent methionine synthase (MetH) is a modular protein that catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine to produce methionine and tetrahydrofolate. The cobalamin cofactor, which serves as both acc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7089525cf0b6689193ca74e5a3bee58
https://doi.org/10.1073/pnas.0906132106
https://doi.org/10.1073/pnas.0906132106
Autor:
Katherine A. Pattridge, Sha Huang, Rowena G. Matthews, Martha L. Ludwig, Gail Romanchuk, Ian A. Wilson, Scott A. Lesley
Publikováno v:
Protein Science. 16:1588-1595
The crystal structure of the Thermotoga maritima gene product TM0269, determined as part of genome-wide structural coverage of T. maritima by the Joint Center for Structural Genomics, revealed structural homology with the fourth module of the cobalam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68dbee1d5af8b43e805b010a6291d11b
https://doi.org/10.1110/ps.072936307
https://doi.org/10.1110/ps.072936307
Autor:
Christian Weber, Jon A. Friesen, Katherine A. Pattridge, Martha L. Ludwig, Claudia Kent, Subramaniam Sanker
Publikováno v:
Journal of Biological Chemistry. 278:51863-51871
The bacterial enzyme, glycerol-3-phosphate cytidylyltransferase (GCT), is a model for mammalian cytidylyltransferases and is a member of a large superfamily of nucleotidyltransferases. Dimeric GCT from Bacillus subtilis displays unusual negative coop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a89926934d570f3ba955ca55ccc6ee1
https://doi.org/10.1074/jbc.m306174200
https://doi.org/10.1074/jbc.m306174200
Autor:
Katherine A. Pattridge, Vahe Bandarian, Brett W. Lennon, Rowena G. Matthews, Donald P. Huddler, Martha L. Ludwig
Publikováno v:
Nature Structural Biology. 9:53-56
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three diffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a034045e712b57dff79ab9f38251eb
https://doi.org/10.1038/nsb738
https://doi.org/10.1038/nsb738
Autor:
Anita L. Metzger, Christian Weber, Catherine L. Drennan, Katherine A. Pattridge, David M. Hoover, Martha L. Ludwig
Publikováno v:
Journal of Molecular Biology. 294:711-724
Flavodoxin from Anacystis nidulans ( Synechococcus PCC 7942) was the first member of the flavodoxin family to be characterized, and is the structural prototype for the “long-chain” flavodoxins that have molecular masses of ∼20 kDa. Crystal stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8be80a90613f2dfc4eddb8953399e083
https://doi.org/10.1006/jmbi.1999.3151
https://doi.org/10.1006/jmbi.1999.3151
Autor:
Catherine L. Drennan, Martha L. Ludwig, Christian Weber, Anita L. Metzger, David M. Hoover, Charles Osborne, Katherine A. Pattridge
Publikováno v:
Journal of Molecular Biology. 294:725-743
The long-chain flavodoxins, with 169-176 residues, display oxidation-reduction potentials at pH 7 that vary from -50 to -260 mV for the oxidized/semiquinone (ox/sq) equilibrium and are -400 mV or lower for the semiquinone/hydroquinone (sq/hq) equilib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74b085afca04c116c279854607ab059e
https://doi.org/10.1006/jmbi.1999.3152
https://doi.org/10.1006/jmbi.1999.3152
Autor:
Katherine A. Pattridge, Melinda M. Dixon, Martha L. Ludwig, Anita L. Metzger, Mesut Eren, Richard P. Swenson, Yucheng Feng
Publikováno v:
Biochemistry. 36:1259-1280
X-ray analyses of wild-type and mutant flavodoxins from Clostridium beijerinckii show that the conformation of the peptide Gly57-Asp58, in a bend near the isoalloxazine ring of FMN, is correlated with the oxidation state of the FMN prosthetic group.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c75448ffba521a98242ed8bb5d1c53
https://doi.org/10.1021/bi962180o
https://doi.org/10.1021/bi962180o
Publikováno v:
Journal of Molecular Biology. 219:335-358
The structure of Mn(III) superoxide dismutase (Mn(III)SOD) from Thermus thermophilus, a tetramer of chains 203 residues in length, has been refined by restrained least-squares methods. The R-factor (= ∑¦¦Fo¦−¦Fc¦¦∑¦Fo¦) for the 54,056 u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36ccef9e4c2d78aa009b82f6dffc3954
https://doi.org/10.1016/0022-2836(91)90569-r
https://doi.org/10.1016/0022-2836(91)90569-r
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 105(11)
B 12 -dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that is alternately methylated by methyltetrahydrofolate to form methylcobalamin and demethylated by homocysteine to form cob(I)alamin. Major domain rearrange
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cf817afaa770d195803ced1ba660613
https://pubmed.ncbi.nlm.nih.gov/18332423
https://pubmed.ncbi.nlm.nih.gov/18332423
Autor:
Martha L. Ludwig, Vincent Massey, Katherine A. Pattridge, Anita L. Metzger, Lawrence M. Schopfer
Publikováno v:
Biochemistry. 29:10364-10375
Flavodoxins from Clostridium beijerinckii and from Megasphaera elsdenii with 1-carba-1-deaza-FMN substituted for FMN have been used to study flavin-protein interactions in flavodoxins. The oxidized 1-deaza analogue of FMN binds to apoflavodoxins from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27d6c1ce37f9d7e1c7b9372e16a64d0e
https://doi.org/10.1021/bi00497a011
https://doi.org/10.1021/bi00497a011