2zgi
Crystal Structure of Putative 4-amino-4-deoxychorismate lyaseCrystal Structure of Putative 4-amino-4-deoxychorismate lyase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe pyridoxal 5'-phosphate-dependent enzyme 4-amino-4-deoxychorismate lyase converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate in one of the crucial steps in the folate-biosynthesis pathway. The primary structure of the hypothetical protein TTHA0621 from Thermus thermophilus HB8 suggests that TTHA0621 is a putative 4-amino-4-deoxychorismate lyase. Here, the crystal structure of TTHA0621 is reported at 1.93 A resolution. The asymmetric unit contained four NCS molecules related by 222 noncrystallographic symmetry, in which the formation of intact dimers may be functionally important. The cofactor pyridoxal 5'-phosphate (PLP) binds to the protein in the large cleft formed by the N-terminal and C-terminal domains of TTHA0621. The high structural similarity and the conservation of the functional residues in the catalytic region compared with 4-amino-4-deoxychorismate lyase (PabC; EC 4.1.3.38) from Escherichia coli suggest that the TTHA0621 protein may also possess 4-amino-4-deoxychorismate lyase activity. Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8.,Padmanabhan B, Bessho Y, Ebihara A, Antonyuk SV, Ellis MJ, Strange RW, Kuramitsu S, Watanabe N, Hasnain SS, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1234-9. Epub 2009 Nov 27. PMID:20054118[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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