2du2
From Proteopedia
(New page: 200px<br /><applet load="2du2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2du2, resolution 2.1Å" /> '''Crystal Structure Ana...) |
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==Overview== | ==Overview== | ||
| - | L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the | + | L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the alpha-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical alpha(8)/beta(8) motif commonly found in other flavin family proteins. A related enzyme, glycolate oxidase, catalyzes the oxidation of glycolate rather than lactate. Comparison of the two enzyme structures highlights the importance of five residues around the FMN prosthetic group of LOX, which act synergistically to discriminate between the l/d configurations of lactate. X-ray crystallography of LOX gave a space group I422 of unit-cell parameters a=b=191.096A, c=194.497A and alpha=beta=gamma=90 degrees with four monomers per asymmetric unit. The four independent monomers display slight structural differences around the active site. Diffraction data were collected, under cryogenic conditions to 2.1A resolution at the synchrotron facilities in Japan. |
==About this Structure== | ==About this Structure== | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:41 2008'' |
Revision as of 15:02, 21 February 2008
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Crystal Structure Analysis of the L-Lactate Oxidase
Overview
L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the alpha-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical alpha(8)/beta(8) motif commonly found in other flavin family proteins. A related enzyme, glycolate oxidase, catalyzes the oxidation of glycolate rather than lactate. Comparison of the two enzyme structures highlights the importance of five residues around the FMN prosthetic group of LOX, which act synergistically to discriminate between the l/d configurations of lactate. X-ray crystallography of LOX gave a space group I422 of unit-cell parameters a=b=191.096A, c=194.497A and alpha=beta=gamma=90 degrees with four monomers per asymmetric unit. The four independent monomers display slight structural differences around the active site. Diffraction data were collected, under cryogenic conditions to 2.1A resolution at the synchrotron facilities in Japan.
About this Structure
2DU2 is a Single protein structure of sequence from Aerococcus viridans with as ligand. Active as Lactate 2-monooxygenase, with EC number 1.13.12.4 Full crystallographic information is available from OCA.
Reference
The crystal structure of L-lactate oxidase from Aerococcus viridans at 2.1A resolution reveals the mechanism of strict substrate recognition., Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y, Biochem Biophys Res Commun. 2006 Nov 17;350(2):249-56. Epub 2006 Sep 18. PMID:17007814
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