1MZV

Crystal Structure of Adenine Phosphoribosyltransferase (APRT) From Leishmania tarentolae

1MZV の概要

• エントリーDOI: 10.2210/pdb1mzv/pdb
• 関連するPDBエントリー: 1qb7
• 分子名称: Adenine Phosphoribosyltransferase, PHOSPHATE ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: alpha/beta structure, transferase
• 由来する生物種: Leishmania tarentolae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26356.02

構造登録者

Thiemann, O.H.,Silva, M.,Oliva, G.,Silva, C.H.T.P.,Iulek, J. (登録日: 2002-10-10, 公開日: 2003-10-28, 最終更新日: 2024-02-14)

主引用文献

Silva, M.,Silva, C.H.T.P.,Iulek, J.,Oliva, G.,Thiemann, O.H.
Crystal structure of adenine phosphoribosyltransferase from Leishmania tarentolae: potential implications for APRT catalytic mechanism.
Biochim.Biophys.Acta, 1696:31-39, 2004

PubMed Abstract: The three-dimensional structure of Leishmania tarentolae adenine phosphoribosyltransferase (APRT) in complex with adenosine-5-monophosphate (AMP) and a phosphate ion has been solved. Refinement against X-ray diffraction data extending to 2.2-A resolution led to a final crystallographic R factor of 18.3%. Structural comparisons amongst this APRT enzyme and other 'type I' PRTases whose structures have been determined reveal several important features of the PRTases catalytic mechanism. Based on structural superpositions and molecular interaction potential calculations, it was possible to suggest that the PRPP is the first substrate to bind, while the AMP is the last product to leave the active site, in accordance to recent kinetic studies performed with the Leishmania donovani APRT.

PubMed: 14726202
DOI: 10.1016/j.bbapap.2003.09.003

実験手法

X-RAY DIFFRACTION (2.2 Å)