Ontology highlight
ABSTRACT:
SUBMITTER: Abad-Zapatero C
PROVIDER: S-EPMC2143388 | biostudies-other | 1996 Apr
REPOSITORIES: biostudies-other
Abad-Zapatero C C Goldman R R Muchmore S W SW Hutchins C C Stewart K K Navaza J J Payne C D CD Ray T L TL
Protein science : a publication of the Protein Society 19960401 4
The three-dimensional structure of a secreted aspartic protease from Candida albicans complexed with a potent inhibitor reveals variations on the classical aspartic protease theme that dramatically alter the specificity of this class of enzymes. The structure presents: (1) an 8-residue insertion near the first disulfide (Cys 45-Cys 50, pepsin numbering) that results in a broad flap extending toward the active site; (2) a 7-residue deletion replacing helix hN2 (Ser 110-Tyr 114), which enlarges th ...[more]