1bqa
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(New page: 200px<br /> <applet load="1bqa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqa, resolution 2.1Å" /> '''ASPARTATE AMINOTRANS...)
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Revision as of 17:54, 29 October 2007
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ASPARTATE AMINOTRANSFERASE P195A MUTANT
Overview
To elucidate the role of the two conserved cis-proline residues of, aspartate aminotransferase (AspAT), one double and two single mutants of, the enzyme from Escherichia coli (EcAspAT) were prepared: P138A, P195A and, P138A/P195A in which the two prolines were replaced by alanine. The, crystal structures of P195A and P138A/P195A have been determined at, 2.3-2.1 A resolution. The wild-type geometry, including the cis, conformation of the 194-195 peptide bond is retained upon substitution of, proline 195 by alanine, whereas the trans conformation is adopted at the, 137-138 peptide bond. Quite surprisingly, the replacement of each of the, two prolines by alanine does not significantly affect either the activity, or the stability of the protein. All the three mutants follow the same, pathway ... [(full description)]
About this Structure
1BQA is a [Single protein] structure of sequence from [Escherichia coli]. Active as [[1]], with EC number [2.6.1.1]. Full crystallographic information is available from [OCA].
Reference
Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase., Birolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G, Biochemistry. 1999 Jan 19;38(3):905-13. PMID:9893985
Page seeded by OCA on Mon Oct 29 19:59:36 2007
