1ket: Difference between revisions
New page: left|200px<br /><applet load="1ket" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ket, resolution 1.80Å" /> '''The crystal structur... |
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[[Image:1ket.jpg|left|200px]]<br /><applet load="1ket" size=" | [[Image:1ket.jpg|left|200px]]<br /><applet load="1ket" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ket, resolution 1.80Å" /> | caption="1ket, resolution 1.80Å" /> | ||
'''The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with thymidine diphosphate bound'''<br /> | '''The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with thymidine diphosphate bound'''<br /> | ||
==Overview== | ==Overview== | ||
dTDP-D-glucose 4,6-dehydratase (RmlB) was first identified in the | dTDP-D-glucose 4,6-dehydratase (RmlB) was first identified in the L-rhamnose biosynthetic pathway, where it catalyzes the conversion of dTDP-D-glucose into dTDP-4-keto-6-deoxy-D-glucose. The structures of RmlB from Salmonella enterica serovar Typhimurium in complex with substrate deoxythymidine 5'-diphospho-D-glucose (dTDP-D-glucose) and deoxythymidine 5'-diphosphate (dTDP), and RmlB from Streptococcus suis serotype 2 in complex with dTDP-D-glucose, dTDP, and deoxythymidine 5'-diphospho-D-pyrano-xylose (dTDP-xylose) have all been solved at resolutions between 1.8 A and 2.4 A. The structures show that the active sites are highly conserved. Importantly, the structures show that the active site tyrosine functions directly as the active site base, and an aspartic and glutamic acid pairing accomplishes the dehydration step of the enzyme mechanism. We conclude that the substrate is required to move within the active site to complete the catalytic cycle and that this movement is driven by the elimination of water. The results provide insight into members of the SDR superfamily. | ||
==About this Structure== | ==About this Structure== | ||
1KET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis] with TYD and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-glucose_4,6-dehydratase dTDP-glucose 4,6-dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.46 4.2.1.46] Full crystallographic information is available from [http:// | 1KET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis] with <scene name='pdbligand=TYD:'>TYD</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-glucose_4,6-dehydratase dTDP-glucose 4,6-dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.46 4.2.1.46] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KET OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Streptococcus suis]] | [[Category: Streptococcus suis]] | ||
[[Category: dTDP-glucose 4,6-dehydratase]] | [[Category: dTDP-glucose 4,6-dehydratase]] | ||
[[Category: Allard, S | [[Category: Allard, S T.M.]] | ||
[[Category: Allen, A | [[Category: Allen, A G.]] | ||
[[Category: Beis, K.]] | [[Category: Beis, K.]] | ||
[[Category: Giraud, M | [[Category: Giraud, M F.]] | ||
[[Category: Graninger, M.]] | [[Category: Graninger, M.]] | ||
[[Category: Gross, J | [[Category: Gross, J W.]] | ||
[[Category: Hegeman, A | [[Category: Hegeman, A D.]] | ||
[[Category: Messner, P.]] | [[Category: Messner, P.]] | ||
[[Category: Naismith, J | [[Category: Naismith, J H.]] | ||
[[Category: Whitfield, C.]] | [[Category: Whitfield, C.]] | ||
[[Category: NAD]] | [[Category: NAD]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:19 2008'' | ||
Revision as of 14:33, 21 February 2008
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The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with thymidine diphosphate bound
OverviewOverview
dTDP-D-glucose 4,6-dehydratase (RmlB) was first identified in the L-rhamnose biosynthetic pathway, where it catalyzes the conversion of dTDP-D-glucose into dTDP-4-keto-6-deoxy-D-glucose. The structures of RmlB from Salmonella enterica serovar Typhimurium in complex with substrate deoxythymidine 5'-diphospho-D-glucose (dTDP-D-glucose) and deoxythymidine 5'-diphosphate (dTDP), and RmlB from Streptococcus suis serotype 2 in complex with dTDP-D-glucose, dTDP, and deoxythymidine 5'-diphospho-D-pyrano-xylose (dTDP-xylose) have all been solved at resolutions between 1.8 A and 2.4 A. The structures show that the active sites are highly conserved. Importantly, the structures show that the active site tyrosine functions directly as the active site base, and an aspartic and glutamic acid pairing accomplishes the dehydration step of the enzyme mechanism. We conclude that the substrate is required to move within the active site to complete the catalytic cycle and that this movement is driven by the elimination of water. The results provide insight into members of the SDR superfamily.
About this StructureAbout this Structure
1KET is a Single protein structure of sequence from Streptococcus suis with and as ligands. Active as dTDP-glucose 4,6-dehydratase, with EC number 4.2.1.46 Full crystallographic information is available from OCA.
ReferenceReference
Toward a structural understanding of the dehydratase mechanism., Allard ST, Beis K, Giraud MF, Hegeman AD, Gross JW, Wilmouth RC, Whitfield C, Graninger M, Messner P, Allen AG, Maskell DJ, Naismith JH, Structure. 2002 Jan;10(1):81-92. PMID:11796113
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