RESUMO
The surface layer of archaeobacteria protects cells from extreme environments and, in Methanosarcina, may regulate cell adhesion. We identify three domain types that account for the complete architecture of numerous Methanosarcina surface layer proteins (SLPs). We solve the crystal structure for two of these domains, which correspond to the two N-terminal domains of an M. mazei SLP. One domain displays a unique, highly symmetrical, seven-bladed beta propeller fold, and the other belongs to the polycystic kidney disease (PKD) superfamily fold. The third domain is predicted to adopt a beta helix fold. These domains have homologs in metazoan cell surface proteins, suggesting remarkable relationships between domains in archaeal SLPs and metazoan cell surface proteins.
Assuntos
Proteínas Arqueais/química , Proteínas de Membrana/química , Sequência de Aminoácidos , Modelos Moleculares , Dados de Sequência Molecular , Conformação Proteica , Homologia de Sequência de AminoácidosRESUMO
Professional development through specialty certification is positively associated with nurses' increased confidence in clinical skills, commitment to learning, empowerment, and professional credibility. This translates to improved patient outcomes, with higher organizational reimbursement, in addition to nurse retention and job satisfaction. Despite the call for lifelong learning from the Institute of Medicine, certification rates, especially among nurses in direct patient care, remain low. This article provides a three-tiered approach for organizational leaders and administrators of continuing education programs to establish resources and support for nurses seeking specialty certification.