1h94
From Proteopedia
(New page: 200px<br /> <applet load="1h94" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h94, resolution 2.5Å" /> '''COMPLEX OF ACTIVE MU...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H94 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with NAD 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=1.1.1.49 1.1.1.49]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H94 OCA]]. | + | 1H94 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with NAD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]]. Structure known Active Site: NAD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H94 OCA]]. |
==Reference== | ==Reference== | ||
NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes., Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11320304 11320304] | NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes., Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11320304 11320304] | ||
| + | [[Category: Glucose-6-phosphate 1-dehydrogenase]] | ||
[[Category: Leuconostoc mesenteroides]] | [[Category: Leuconostoc mesenteroides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase (choh(d) - nad(p))]] | [[Category: oxidoreductase (choh(d) - nad(p))]] | ||
| - | ''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 14:20:54 2007'' |
Revision as of 12:16, 30 October 2007
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COMPLEX OF ACTIVE MUTANT (S215->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L.MESENTEROIDES WITH COENZYME NAD
Overview
The reduced coenzymes NADH and NADPH only differ by one phosphate, but in, the cell NADH provides reducing power for catabolism while NADPH is, utilized in biosynthetic pathways. Enzymes almost invariably discriminate, between the coenzymes, but glucose 6-phosphate dehydrogenase (G6PD) from, Leuconostoc mesenteroides is rare in being functionally dual specific. In, order to elucidate the coenzyme selectivity, the structures of NADP(+)-, and NAD(+)-complexed L. mesenteroides G6PD have been determined including, data to 2.2 and 2.5 A resolution, respectively, and compared with, unliganded G6PD crystallized in the same space groups. Coenzyme binding is, also compared with that in a ternary complex of a mutant in which Asp177, in the active site has been mutated to asparagine. There are no ... [(full description)]
About this Structure
1H94 is a [Single protein] structure of sequence from [Leuconostoc mesenteroides] with NAD as [ligand]. Active as [Glucose-6-phosphate 1-dehydrogenase], with EC number [1.1.1.49]. Structure known Active Site: NAD. Full crystallographic information is available from [OCA].
Reference
NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes., Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:11320304
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