1KHD

Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum)

1KHD の概要

• エントリーDOI: 10.2210/pdb1khd/pdb
• 関連するPDBエントリー: 1KGZ
• 分子名称: Anthranilate phosphoribosyltransferase (2 entities in total)
• 機能のキーワード: type 3 prt fold, nucleotide binding fold, transferase
• 由来する生物種: Pectobacterium carotovorum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 148228.47

構造登録者

Kim, C.,Xuong, N.-H.,Edwards, S.,Madhusudan,Yee, M.-C.,Spraggon, G.,Mills, S.E. (登録日: 2001-11-29, 公開日: 2002-10-23, 最終更新日: 2023-08-16)

主引用文献

Kim, C.,Xuong, N.-H.,Edwards, S.,Madhusudan,Yee, M.-C.,Spraggon, G.,Mills, S.E.
The Crystal Structure of Anthranilate Phosphoribosyltransferase from the Enterobacterium Pectobacterium carotovorum
FEBS Lett., 523:239-246, 2002

PubMed Abstract: The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known.

PubMed: 12123839
DOI: 10.1016/S0014-5793(02)02905-8

実験手法

X-RAY DIFFRACTION (1.86 Å)