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Modeling Protein Flexibility for Structure-Based (2002)
| Content Provider | CiteSeerX |
|---|---|
| Author | Redesign, Active Site Lilien, Ryan H. Anderson, Amy C. Donald, Bruce R. |
| Description | Introduction A variety of microorganisms synthesize modified peptide-like products using enzymes called NonRibosomal Peptide Synthetases (NRPS). Each NRPS protein synthesizes a specific product using multiple domains in an assembly-line fashion. These products are pharmaceutically active and include many antibiotics, antifungals, and immunosuppressants. Synthesis is initiated with the binding of an amino acid X to an adenylation (A) domain; an aminoacyl-adenylate (X-AMP) is formed and transferred down the assembly line. We consider the engineering problem of switching the specificity of an NRPS from its natural substrate to a new amino acid substrate using computational structural modeling techniques, in hopes of producing novel NRPS products. We hope to increase the e#ciency and success rate of current protein redesign e#orts. We will modify the NRPS enzyme gramicidin S synthetase A (GrsA), for which we have genetic sequence and structural data for the Phe A domain [6]. 2 Methods O |
| File Format | |
| Language | English |
| Publisher Date | 2002-01-01 |
| Publisher Institution | Intl. Conf. on Research in Comput. Mol. Biol. (RECOMB) in Currents in Computational Molecular Biology 2002 |
| Access Restriction | Open |
| Subject Keyword | Phe Domain Computational Structural Modeling Technique Nrps Protein Amino Acid Peptide-like Product New Amino Acid Substrate Novel Nrps Product Genetic Sequence Protein Flexibility Current Protein Redesign Orts Nonribosomal Peptide Synthetases Assembly Line Structural Data Multiple Domain Specific Product Nrps Enzyme Gramicidin Synthetase Many Antibiotic Natural Substrate Success Rate Engineering Problem Assembly-line Fashion |
| Content Type | Text |
| Resource Type | Article |
