5C9B

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

Summary for 5C9B

• Entry DOI: 10.2210/pdb5c9b/pdb
• Related: 5C9D 5C9F
• Descriptor: ApRick protease (2 entities in total)
• Functional Keywords: pepsin, aprick, hydrolase
• Biological source: Rickettsia conorii
• Total number of polymer chains: 4
• Total formula weight: 63451.22

Authors

Li, M.,Gustchina, A.,Cruz, R.,Simoes, M.,Curto, P.,Martinez, J.,Faro, C.,Simoes, I.,Wlodawer, A. (deposition date: 2015-06-26, release date: 2015-10-14, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)