A mutant D-amino acid aminotransferase with broad substrate specificity: construction by replacement of the interdomain loop Pro119- Arg120-Pro121 by Gly-Gly-Gly
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چکیده
منابع مشابه
Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase.
The regulatory and substrate binding domains of D-3-phosphoglycerate dehydrogenase (PGDH, EC 1.1.1.95) from Escherichia coli are connected by a single polypeptide strand that contains a Gly-Gly sequence approximately midway between the domains. The potential flexibility of this sequence and its strategic location between major domain structures suggests that it may function in the conformationa...
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Li(+) and Ca(2+) binding to the carbonyl oxygen sites of a model peptide system has been studied by (17)O solid-state NMR spectroscopy. (17)O chemical shift (CS) and quadrupole coupling (QC) tensors are determined in four Gly-(Gly-(17)O)-Gly polymorphs by a combination of stationary and fast magic-angle spinning (MAS) methods at high magnetic field, 19.6 T. In the crystal lattice, the carbonyl ...
متن کاملThe tripeptide N-Cbz-βGly-Gly-Gly-Obz
The title peptide, N-benzyl-oxycarbonyl-β-glycylglycylglycine benzyl ester, C22H25N3O6, contains a non-proteinogenic amino acid residue, β-glycine, which is a homologated analogue of glycine. In the mol-ecular structure, β-glycine adopts an extended conformation with a trans conformation about its C(β)-C(α) bond. The second glycine residue adopts an extended conformation while the third glycine...
متن کاملInfrared Spectroscopy of Mobility-Selected H+-Gly-Pro-Gly-Gly (GPGG).
We report the first results from a new instrument capable of acquiring infrared spectra of mobility-selected ions. This demonstration involves using ion mobility to first separate the protonated peptide Gly-Pro-Gly-Gly (GPGG) into two conformational families with collisional cross-sections of 93.8 and 96.8 Å(2). After separation, each family is independently analyzed by acquiring the infrared p...
متن کاملSecondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk
Solid-state NMR and molecular dynamics (MD) simulations are presented to help elucidate the molecular secondary structure of poly(Gly-Gly-X), which is one of the most common structural repetitive motifs found in orb-weaving dragline spider silk proteins. The combination of NMR and computational experiments provides insight into the molecular secondary structure of poly(Gly-Gly-X) segments and p...
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ژورنال
عنوان ژورنال: Protein Engineering Design and Selection
سال: 1998
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/11.1.53