1NH7

ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS

1NH7 の概要

• エントリーDOI: 10.2210/pdb1nh7/pdb
• 関連するPDBエントリー: 1NH8
• 分子名称: ATP Phosphoribosyltransferase, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: prtase, de novo his biosynthesis, prpp, transferase, phosphoribosyltransferase, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• 細胞内の位置: Cytoplasm (By similarity): P60759
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33188.69

構造登録者

Cho, Y.,Sharma, V.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 2002-12-18, 公開日: 2003-02-11, 最終更新日: 2024-12-25)

主引用文献

Cho, Y.,Sharma, V.,Sacchettini, J.C.
Crystal Structure of ATP Phosphoribosyltransferase from Mycobacterium Tuberculosis
J.Biol.Chem., 278:8333-, 2003

PubMed Abstract: The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of the histidine biosynthetic pathway and is regulated by a feedback mechanism by the product histidine. The crystal structures of the N-1-(5'-phosphoribosyl)-ATP transferase from Mycobacterium tuberculosis in complex with inhibitor histidine and AMP has been determined to 1.8 A resolution and without ligands to 2.7 A resolution. The active enzyme exists primarily as a dimer, and the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of three continuous domains. The inhibitor AMP binds in the active site cavity formed between the two catalytic domains. A model for the mechanism of allosteric inhibition has been derived from conformational differences between the AMP:His-bound and apo structures.

PubMed: 12511575
DOI: 10.1074/jbc.M212124200

実験手法

X-RAY DIFFRACTION (2.7 Å)