1geg
From Proteopedia
(New page: 200px<br /><applet load="1geg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1geg, resolution 1.7Å" /> '''CRYATAL STRUCTURE ANA...) |
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| - | [[Image:1geg.jpg|left|200px]]<br /><applet load="1geg" size=" | + | [[Image:1geg.jpg|left|200px]]<br /><applet load="1geg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1geg, resolution 1.7Å" /> | caption="1geg, resolution 1.7Å" /> | ||
'''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE'''<br /> | '''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a ternary complex of meso-2,3-butanediol | + | The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 A resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, Gln140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate. |
==About this Structure== | ==About this Structure== | ||
| - | 1GEG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with GLC, MG, NAD and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetoin_dehydrogenase Acetoin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.5 1.1.1.5] Full crystallographic information is available from [http:// | + | 1GEG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetoin_dehydrogenase Acetoin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.5 1.1.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEG OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms., Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M, J Biochem | + | Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms., Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M, J Biochem. 2001 Feb;129(2):205-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11173520 11173520] |
[[Category: Acetoin dehydrogenase]] | [[Category: Acetoin dehydrogenase]] | ||
[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
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[[Category: sdr family]] | [[Category: sdr family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:11 2008'' |
Revision as of 10:49, 21 February 2008
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CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE
Overview
The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 A resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, Gln140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.
About this Structure
1GEG is a Single protein structure of sequence from Klebsiella pneumoniae with , , and as ligands. Active as Acetoin dehydrogenase, with EC number 1.1.1.5 Full crystallographic information is available from OCA.
Reference
Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms., Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M, J Biochem. 2001 Feb;129(2):205-8. PMID:11173520
Page seeded by OCA on Thu Feb 21 12:49:11 2008
Categories: Acetoin dehydrogenase | Klebsiella pneumoniae | Single protein | Kurisu, G. | Kusunoki, M. | Otagiri, M. | Ui, S. | BME | GLC | MG | NAD | Sdr family
