5c9b

Publication Abstract from PubMed

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.

Structure of RC1339/APRc from Rickettsia conorii, a retropepsin-like aspartic protease.,Li M, Gustchina A, Cruz R, Simoes M, Curto P, Martinez J, Faro C, Simoes I, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):2109-18. doi:, 10.1107/S1399004715013905. Epub 2015 Sep 30. PMID:26457434^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.