5C9F

Crystal structure of a retropepsin-like aspartic protease from Rickettsia conorii

5C9F の概要

• エントリーDOI: 10.2210/pdb5c9f/pdb
• 関連するPDBエントリー: 5C9B 5C9D
• 分子名称: ApRick protease, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: pepsin, aprick, hydrolase
• 由来する生物種: Rickettsia conorii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63382.87

構造登録者

Li, M.,Gustchina, A.,Cruz, R.,Simoes, M.,Curto, P.,Martinez, J.,Faro, C.,Simoes, I.,Wlodawer, A. (登録日: 2015-06-26, 公開日: 2015-10-14, 最終更新日: 2024-03-06)

主引用文献

Li, M.,Gustchina, A.,Cruz, R.,Simoes, M.,Curto, P.,Martinez, J.,Faro, C.,Simoes, I.,Wlodawer, A.
Structure of RC1339/APRc from Rickettsia conorii, a retropepsin-like aspartic protease.
Acta Crystallogr. D Biol. Crystallogr., 71:2109-2118, 2015

PubMed Abstract: The crystal structures of two constructs of RC1339/APRc from Rickettsia conorii, consisting of either residues 105-231 or 110-231 followed by a His tag, have been determined in three different crystal forms. As predicted, the fold of a monomer of APRc resembles one-half of the mandatory homodimer of retroviral pepsin-like aspartic proteases (retropepsins), but the quaternary structure of the dimer of APRc differs from that of the canonical retropepsins. The observed dimer is most likely an artifact of the expression and/or crystallization conditions since it cannot support the previously reported enzymatic activity of this bacterial aspartic protease. However, the fold of the core of each monomer is very closely related to the fold of retropepsins from a variety of retroviruses and to a single domain of pepsin-like eukaryotic enzymes, and may represent a putative common ancestor of monomeric and dimeric aspartic proteases.

PubMed: 26457434
DOI: 10.1107/S1399004715013905

実験手法

X-RAY DIFFRACTION (2 Å)