2dab
From Proteopedia
(New page: 200px<br /> <applet load="2dab" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dab, resolution 2.0Å" /> '''L201A MUTANT OF D-AM...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2DAB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]] with PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]]. | + | 2DAB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]] with PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21]]. Structure known Active Sites: ASA and ASB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DAB OCA]]. |
==Reference== | ==Reference== | ||
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination., Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N, Protein Eng. 1998 Aug;11(8):613-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9749913 9749913] | Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination., Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N, Protein Eng. 1998 Aug;11(8):613-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9749913 9749913] | ||
[[Category: Bacillus sp.]] | [[Category: Bacillus sp.]] | ||
| + | [[Category: D-amino-acid transaminase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Esaki, N.]] | [[Category: Esaki, N.]] | ||
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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 13:46:56 2007'' |
Revision as of 11:42, 30 October 2007
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L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE
Overview
The leucine-to-alanine mutation at residue 201 of D-amino acid, aminotransferase provides a unique enzyme which gradually loses its, activity while catalyzing the normal transamination; the co-enzyme form is, converted from pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate upon, the inactivation [Kishimoto,K., Yoshimura,T., Esaki,N., Sugio,S., Manning,J.M. and Soda,K. (1995) J. Biochem., 117, 691-696]. Crystal, structures of both co-enzyme forms of the mutant enzyme have been, determined at 2.0 A resolution: they are virtually identical, and are, quite similar to that of the wild-type enzyme. Significant differences in, both forms of the mutant are localized only on the bound co-enzyme, the, side chains of Lys145 and Tyr31, and a water molecule sitting on the, putative substrate binding ... [(full description)]
About this Structure
2DAB is a [Single protein] structure of sequence from [Bacillus sp.] with PLP as [ligand]. Active as [D-amino-acid transaminase], with EC number [2.6.1.21]. Structure known Active Sites: ASA and ASB. Full crystallographic information is available from [OCA].
Reference
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination., Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N, Protein Eng. 1998 Aug;11(8):613-9. PMID:9749913
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