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5M1E

Crystal structure of N-terminally tagged UbiD from E. coli reconstituted with prFMN cofactor

Summary for 5M1E
Entry DOI10.2210/pdb5m1e/pdb
Descriptor3-octaprenyl-4-hydroxybenzoate carboxy-lyase, MANGANESE (II) ION, (16~{R})-11,12,14,14-tetramethyl-3,5-bis(oxidanylidene)-8-[(2~{S},3~{S},4~{R})-2,3,4-tris(oxidanyl)-5-phosphonooxy-pentyl]-1,4,6,8-tetrazatetracyclo[7.7.1.0^{2,7}.0^{13,17}]heptadeca-2(7),9(17),10,12-tetraene-16-sulfonic acid, ... (5 entities in total)
Functional Keywordsubid, decarboxylase, ubiquinone biosynthesis, prfmn binding, lyase
Biological sourceEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Cellular locationCell membrane ; Peripheral membrane protein : P0AAB5
Total number of polymer chains3
Total formula weight175563.91
Authors
Marshall, S.A.,Leys, D. (deposition date: 2016-10-07, release date: 2017-01-11, Last modification date: 2024-01-17)
Primary citationMarshall, S.A.,Fisher, K.,Ni Cheallaigh, A.,White, M.D.,Payne, K.A.,Parker, D.A.,Rigby, S.E.,Leys, D.
Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.
J. Biol. Chem., 292:4623-4637, 2017
Cited by
PubMed: 28057757
DOI: 10.1074/jbc.M116.762732
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.62 Å)
Structure validation

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