2B3L

Crystal structure of type I human methionine aminopeptidase in the apo form

2B3L の概要

• エントリーDOI: 10.2210/pdb2b3l/pdb
• 関連するPDBエントリー: 2B3H 2B3K
• 分子名称: Methionine aminopeptidase 1, POTASSIUM ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: methionine aminopeptidase, human, hydrolase, metalloprotease, pitabread fold
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P53582
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37219.26

構造登録者

Addlagatta, A.,Hu, X.,Liu, J.O.,Matthews, B.W. (登録日: 2005-09-20, 公開日: 2005-11-22, 最終更新日: 2023-08-23)

主引用文献

Addlagatta, A.,Hu, X.,Liu, J.O.,Matthews, B.W.
Structural Basis for the Functional Differences between Type I and Type II Human Methionine Aminopeptidases(,).
Biochemistry, 44:14741-14749, 2005

PubMed Abstract: Determination of the crystal structure of human MetAP1 makes it possible, for the first time, to compare the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from the same organism. Comparison of the Type I enzyme with the previously reported complex of ovalicin with Type II MetAP shows that the active site of the former is reduced in size and would incur steric clashes with the bound inhibitor. This explains why ovalicin and related anti-angiogenesis inhibitors target Type II human MetAP but not Type I. The differences in both size and shape of the active sites between MetAP1 and MetAP2 also help to explain their different substrate specificity. In the presence of excess Co(2+), a third cobalt ion binds in the active site region, explaining why metal ions in excess can be inhibitory. Also, the N-terminal region of the protein contains three distinct Pro-x-x-Pro motifs, supporting the prior suggestion that this region of the protein may participate in binding to the ribosome.

PubMed: 16274222
DOI: 10.1021/bi051691k

実験手法

X-RAY DIFFRACTION (1.5 Å)