2ZGI

Crystal Structure of Putative 4-amino-4-deoxychorismate lyase

Summary for 2ZGI

• Entry DOI: 10.2210/pdb2zgi/pdb
• Descriptor: Putative 4-amino-4-deoxychorismate lyase, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE, ... (6 entities in total)
• Functional Keywords: ttha0621, plp cofactor, pyridoxal enzyme, lyase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Thermus thermophilus
• Total number of polymer chains: 4
• Total formula weight: 111341.89

Authors

Padmanabhan, B.,Bessho, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2008-01-22, release date: 2008-07-22, Last modification date: 2025-03-26)

Primary citation

Padmanabhan, B.,Bessho, Y.,Ebihara, A.,Antonyuk, S.V.,Ellis, M.J.,Strange, R.W.,Kuramitsu, S.,Watanabe, N.,Hasnain, S.S.,Yokoyama, S.
Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8.
Acta Crystallogr.,Sect.F, 65:1234-1239, 2009

PubMed Abstract: The 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.

PubMed: 20054118
DOI: 10.1107/S1744309109050052

Experimental method

X-RAY DIFFRACTION (1.93 Å)