Molecular architecture of the ATP-dependent CodWX protease having an N-terminal serine active site

• Published in: The EMBO journal Vol. 22; no. 12; pp. 2893 - 2902
• Main Authors: Cheong, Gang-Won, Chung, Chin Ha, Kang, Min Suk, Kim, Soon Rae, Kwack, Pyeongsu, Lim, Byung Kook, Ahn, Sung Won, Rho, Young Min, Seong, Ihn Sik, Park, Seong-Chul, Eom, Soo Hyun
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 16.06.2003; Blackwell Publishing Ltd; Oxford University Press
• Subjects: Adenosine Triphosphate - metabolism; ATP-dependent protease; ATP-Dependent Proteases; Bacillus subtilis; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding Sites; CodWX; EzrA; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - metabolism; HslVU; Macromolecular Substances; N-terminal serine protease; Protein Structure, Quaternary; Serine - chemistry; Serine - metabolism; Serine Endopeptidases - chemistry; Serine Endopeptidases - metabolism; Serine Endopeptidases - ultrastructure
• ISSN: 0261-4189; 1460-2075; 1460-2075
• DOI: 10.1093/emboj/cdg289

CodWX in Bacillus subtilis is an ATP‐dependent, N‐terminal serine protease, consisting of CodW peptidase and CodX ATPase. Here we show that CodWX is an alkaline protease and has a distinct molecular architecture. ATP hydrolysis is required for the formation of the CodWX complex and thus for its proteolytic function. Remarkably, CodX has a ‘spool‐like’ structure that is formed by interaction of the intermediate domains of two hexameric or heptameric rings. In the CodWX complex, CodW consisting of two stacked hexameric rings (WW) binds to either or both ends of a CodX double ring (XX), forming asymmetric (WWXX) or symmetric cylindrical particles (WWXXWW). CodWX can also form an elongated particle, in which an additional CodX double ring is bound to the symmetric particle (WWXXWWXX). In addition, CodWX is capable of degrading EzrA, an inhibitor of FtsZ ring formation, implicating it in the regulation of cell division. Thus, CodWX appears to constitute a new type of protease that is distinct from other ATP‐dependent proteases in its structure and proteolytic mechanism.