1bqa
From Proteopedia
(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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==About this Structure== | ==About this Structure== | ||
| - | 1BQA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BQA OCA]]. | + | 1BQA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]]. Structure known Active Sites: ACT and BCT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BQA OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9893985 9893985] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9893985 9893985] | ||
| + | [[Category: Aspartate transaminase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:58:27 2007'' |
Revision as of 10:53, 30 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 [Aspartate transaminase], with EC number [2.6.1.1]. Structure known Active Sites: ACT and BCT. 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
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