2j3j: Difference between revisions
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==Overview== | ==Overview== | ||
In this study, we determined the crystal structures of the apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond, reductase encoded by At5g16970. This protein, one of 11 homologues in, Arabidopsis thaliana, is most closely related to the Pinus taeda, phenylpropenal double bond reductase, involved in, for example, heartwood, formation. Both enzymes also have essential roles in plant defense, and, can function by catalyzing the reduction of the 7-8-double bond of, phenylpropanal substrates, such as p-coumaryl and coniferyl aldehydes in, vitro. At5g16970 is also capable of reducing toxic substrates with the, same alkenal functionality, such as 4-hydroxy-(2E)-nonenal. The overall, fold of At5g16970 is similar to that of the zinc-independent medium chain, ... | In this study, we determined the crystal structures of the apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond, reductase encoded by At5g16970. This protein, one of 11 homologues in, Arabidopsis thaliana, is most closely related to the Pinus taeda, phenylpropenal double bond reductase, involved in, for example, heartwood, formation. Both enzymes also have essential roles in plant defense, and, can function by catalyzing the reduction of the 7-8-double bond of, phenylpropanal substrates, such as p-coumaryl and coniferyl aldehydes in, vitro. At5g16970 is also capable of reducing toxic substrates with the, same alkenal functionality, such as 4-hydroxy-(2E)-nonenal. The overall, fold of At5g16970 is similar to that of the zinc-independent medium chain, dehydrogenase/reductase superfamily, the members of which have two domains, and are dimeric in nature, i.e. in contrast to their original, classification as being zinc-containing oxidoreductases. As provisionally, anticipated from the kinetic data, the shape of the binding pocket can, readily accommodate p-coumaryl aldehyde, coniferyl aldehyde, 4-hydroxy-(2E)-nonenal, and 2-alkenals. However, the enzyme kinetic data, among these potential substrates differ, favoring p-coumaryl aldehyde., Tyr-260 is provisionally proposed to function as a general acid/base for, hydride transfer. A catalytic mechanism for this reduction, and its, applicability to related important detoxification mammalian proteins, is, also proposed. | ||
==About this Structure== | ==About this Structure== | ||
2J3J is a | 2J3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAP and HC4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2-alkenal_reductase 2-alkenal reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.74 1.3.1.74] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J3J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ternary complex]] | [[Category: ternary complex]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:07:35 2007'' | ||
