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A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins

Autor: C L, Colbert, M M, Couture, L D, Eltis, J T, Bolin

Publikováno v: Structure (London, England : 1993). 8(12)

Ring-hydroxylating dioxygenases are multicomponent systems that initiate biodegradation of aromatic compounds. Many dioxygenase systems include Rieske-type ferredoxins with amino acid sequences and redox properties remarkably different from the Riesk

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b922db50704151f8ef8d54112b413fc4
https://pubmed.ncbi.nlm.nih.gov/11188691

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Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3

Autor: D, Zhang, A, Kiyatkin, J T, Bolin, P S, Low

Publikováno v: Blood. 96(9)

The red blood cell membrane (RBCM) is a primary model for animal cell plasma membranes. One of its major organizing centers is the cytoplasmic domain of band 3 (cdb3), which links multiple proteins to the membrane. Included among its peripheral prote

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::97f997d80c9c8235b73bf55edf9f0dec
https://pubmed.ncbi.nlm.nih.gov/11049968

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The role of metal clusters and MgATP in nitrogenase catalysis

Autor: L E, Mortenson, L C, Seefeldt, T V, Morgan, J T, Bolin

Publikováno v: Advances in enzymology and related areas of molecular biology. 67

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::725681b7a2c07ffd06c7df7f3d9642fb
https://pubmed.ncbi.nlm.nih.gov/8322617

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High-resolution crystal structures of 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB-degrading bacterium complexed with substrates

Autor: J. T. Bolin, Seungil Han, L. D. Eltis

Publikováno v: Acta Crystallographica Section A Foundations of Crystallography. 52:C129-C129

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f049a032123199750dcda4e333ef2cbc
https://doi.org/10.1107/s0108767396094032

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Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis

Autor: D J, Filman, J T, Bolin, D A, Matthews, J, Kraut

Publikováno v: The Journal of biological chemistry. 257(22)

New details of NADPH binding to Lactobacillus casei dihydrofolate reductase have become visible as a result of crystallographic refinement to an R factor of 0.152 at 1.7 A resolution. Conformational torsion angles for bound NADPH have been extensivel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2ebfa9dbb98ecd0fcf9c0e9174d9209e
https://pubmed.ncbi.nlm.nih.gov/6815179

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Dihydrofolate reductase. The stereochemistry of inhibitor selectivity

Autor: D A, Matthews, J T, Bolin, J M, Burridge, D J, Filman, K W, Volz, J, Kraut

Publikováno v: The Journal of biological chemistry. 260(1)

X-ray structural results are reported for 10 triazine and pyrimidine inhibitors of dihydrofolate reductase, each one studied as a ternary complex with NADPH and chicken dihydrofolate reductase. Analysis of these data and comparison with structural re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5af1ac67f3a98ce62272a49e3d3c4541
https://pubmed.ncbi.nlm.nih.gov/3880743

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Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim

Autor: D A, Matthews, J T, Bolin, J M, Burridge, D J, Filman, K W, Volz, B T, Kaufman, C R, Beddell, J N, Champness, D K, Stammers, J, Kraut

Publikováno v: The Journal of biological chemistry. 260(1)

Refined crystal structures are reported for complexes of Escherichia coli and chicken dihydrofolate reductase containing the antibiotic trimethoprim (TMP). Structural comparison of these two complexes reveals major geometrical differences in TMP bind

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a12e7493134b4913e53b196f97c80dd3
https://pubmed.ncbi.nlm.nih.gov/3880742

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Dihydrofolate reductase from Lactobacillus casei. X-ray structure of the enzyme methotrexate.NADPH complex

Autor: D A, Matthews, R A, Alden, J T, Bolin, D J, Filman, S T, Freer, R, Hamlin, W G, Hol, R L, Kisliuk, E J, Pastore, L T, Plante, N, Xuong, J, Kraut

Publikováno v: The Journal of biological chemistry. 253(19)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::49e5149850c506cbe690383f75345b83
https://pubmed.ncbi.nlm.nih.gov/29045

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Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate

Autor: J T, Bolin, D J, Filman, D A, Matthews, R C, Hamlin, J, Kraut

Publikováno v: The Journal of biological chemistry. 257(22)

X-ray data have been extended to 1.7 A for a binary complex of Escherichia coli dihydrofolate reductase with methotrexate and a ternary complex of Lactobacillus casei dihydrofolate reductase with methotrexate and NADPH. Models for both structures hav

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ddac63b07f4cfe3c9d25b47410636aa5
https://pubmed.ncbi.nlm.nih.gov/6815178

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