1h4j
From Proteopedia
(New page: 200px<br /> <applet load="1h4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4j, resolution 3.0Å" /> '''METHYLOBACTERIUM EXT...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H4J is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens]] with CA and PQQ as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.8 1.1.99.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4J OCA]]. | + | 1H4J is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens]] with CA and PQQ as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(acceptor) Alcohol dehydrogenase (acceptor)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.8 1.1.99.8]]. Structure known Active Sites: AC1, AC2, AC3, AC5, AC6, AC7 and AC8. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4J OCA]]. |
==Reference== | ==Reference== | ||
Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)., Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C, Biochemistry. 2001 Aug 21;40(33):9799-809. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11502173 11502173] | Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)., Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C, Biochemistry. 2001 Aug 21;40(33):9799-809. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11502173 11502173] | ||
| + | [[Category: Alcohol dehydrogenase (acceptor)]] | ||
[[Category: Methylobacterium extorquens]] | [[Category: Methylobacterium extorquens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 26: | Line 27: | ||
[[Category: quinoprotein]] | [[Category: quinoprotein]] | ||
| - | ''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 12:42:45 2007'' |
Revision as of 10:38, 30 October 2007
|
METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE D303E MUTANT
Overview
Two proteins specifically involved in methanol oxidation in the, methylotrophic bacterium Methylobacterium extorquens have been modified by, site-directed mutagenesis. Mutation of the proposed active site base, (Asp303) to glutamate in methanol dehydrogenase (MDH) gave an active, enzyme (D303E-MDH) with a greatly reduced affinity for substrate and with, a lower activation energy. Results of kinetic and deuterium isotope, studies showed that the essential mechanism in the mutant protein was, unchanged, and that the step requiring activation by ammonia remained rate, limiting. No spectrally detectable intermediates could be observed during, the reaction. The X-ray structure, determined to 3 A resolution, of, D303E-MDH showed that the position and coordination geometry of the Ca2+, ion in ... [(full description)]
About this Structure
1H4J is a [Protein complex] structure of sequences from [Methylobacterium extorquens] with CA and PQQ as [ligands]. Active as [Alcohol dehydrogenase (acceptor)], with EC number [1.1.99.8]. Structure known Active Sites: AC1, AC2, AC3, AC5, AC6, AC7 and AC8. Full crystallographic information is available from [OCA].
Reference
Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)., Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C, Biochemistry. 2001 Aug 21;40(33):9799-809. PMID:11502173
Page seeded by OCA on Tue Oct 30 12:42:45 2007
