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New page: left|200px<br /><applet load="1kew" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kew, resolution 1.80Å" /> '''The crystal structur...
 
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[[Image:1kew.jpg|left|200px]]<br /><applet load="1kew" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kew.jpg|left|200px]]<br /><applet load="1kew" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kew, resolution 1.80&Aring;" />
caption="1kew, resolution 1.80&Aring;" />
'''The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar Typhimurium with thymidine diphosphate bound'''<br />
'''The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar Typhimurium with thymidine diphosphate bound'''<br />


==Overview==
==Overview==
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.
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==
1KEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium] with TYD, NAD and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KEW OCA].  
1KEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium] with <scene name='pdbligand=TYD:'>TYD</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=GOL:'>GOL</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=1KEW OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: dTDP-glucose 4,6-dehydratase]]
[[Category: dTDP-glucose 4,6-dehydratase]]
[[Category: Allard, S.T.M.]]
[[Category: Allard, S T.M.]]
[[Category: Allen, A.G.]]
[[Category: Allen, A G.]]
[[Category: Beis, K.]]
[[Category: Beis, K.]]
[[Category: Giraud, M.F.]]
[[Category: Giraud, M F.]]
[[Category: Graninger, M.]]
[[Category: Graninger, M.]]
[[Category: Gross, J.W.]]
[[Category: Gross, J W.]]
[[Category: Hegeman, A.D.]]
[[Category: Hegeman, A D.]]
[[Category: Messner, P.]]
[[Category: Messner, P.]]
[[Category: Naismith, J.H.]]
[[Category: Naismith, J H.]]
[[Category: Whitfield, C.]]
[[Category: Whitfield, C.]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:08:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:28 2008''