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2FWM

Crystal Structure of E. coli EntA, a 2,3-dihydrodihydroxy benzoate dehydrogenase

Summary for 2FWM
Entry DOI10.2210/pdb2fwm/pdb
Descriptor2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (2 entities in total)
Functional Keywordsenterobactin, rossmann fold, chorismate metabolism, short-chain oxidoreductase, tetramer, oxidoreductase
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight26466.78
Authors
Gulick, A.M.,Duax, W.L. (deposition date: 2006-02-02, release date: 2006-06-27, Last modification date: 2024-02-14)
Primary citationSundlov, J.A.,Garringer, J.A.,Carney, J.M.,Reger, A.S.,Drake, E.J.,Duax, W.L.,Gulick, A.M.
Determination of the crystal structure of EntA, a 2,3-dihydro-2,3-dihydroxybenzoic acid dehydrogenase from Escherichia coli.
Acta Crystallogr.,Sect.D, 62:734-740, 2006
Cited by
PubMed Abstract: The Escherichia coli enterobactin synthetic cluster is composed of six proteins, EntA-EntF, that form the enterobactin molecule from three serine molecules and three molecules of 2,3-dihydroxybenzoic acid (DHB). EntC, EntB and EntA catalyze the three-step synthesis of DHB from chorismate. EntA is a member of the short-chain oxidoreductase (SCOR) family of proteins and catalyzes the final step in DHB synthesis, the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoic acid to DHB. The structure of EntA has been determined by multi-wavelength anomalous dispersion methods. Here, the 2.0 A crystal structure of EntA in the unliganded form is presented. Analysis of the structure in light of recent structural and bioinformatic analysis of other members of the SCOR family provides insight into the residues involved in cofactor and substrate binding.
PubMed: 16790929
DOI: 10.1107/S0907444906015824
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

237735

数据于2025-06-18公开中

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