1kc3: Difference between revisions

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New page: left|200px<br /><applet load="1kc3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kc3, resolution 2.70Å" /> '''Crystal structure of...
 
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[[Image:1kc3.jpg|left|200px]]<br /><applet load="1kc3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kc3.jpg|left|200px]]<br /><applet load="1kc3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kc3, resolution 2.70&Aring;" />
caption="1kc3, resolution 2.70&Aring;" />
'''Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose'''<br />
'''Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose'''<br />


==Overview==
==Overview==
dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) catalyzes the final step, in the conversion of dTDP-D-glucose to dTDP-L-rhamnose in an NAD(P)H- and, Mg2+-dependent reaction. L-rhamnose biosynthesis is an antibacterial, target. The structure of RmlD from Salmonella enterica serovar Typhimurium, has been determined, and complexes with NADH, NADPH, and dTDP-L-rhamnose, are reported. RmlD differs from other short chain dehydrogenases in that, it has a novel dimer interface that contains Mg2+. Enzyme catalysis, involves hydride transfer from the nicotinamide ring of the cofactor to, the C4'-carbonyl group of the substrate. The substrate is activated, through protonation by a conserved tyrosine. NAD(P)H is bound in a, solvent-exposed cleft, allowing facile replacement. We suggest a novel, role for the conserved serine/threonine residue of the catalytic triad of, SDR enzymes.
dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) catalyzes the final step in the conversion of dTDP-D-glucose to dTDP-L-rhamnose in an NAD(P)H- and Mg2+-dependent reaction. L-rhamnose biosynthesis is an antibacterial target. The structure of RmlD from Salmonella enterica serovar Typhimurium has been determined, and complexes with NADH, NADPH, and dTDP-L-rhamnose are reported. RmlD differs from other short chain dehydrogenases in that it has a novel dimer interface that contains Mg2+. Enzyme catalysis involves hydride transfer from the nicotinamide ring of the cofactor to the C4'-carbonyl group of the substrate. The substrate is activated through protonation by a conserved tyrosine. NAD(P)H is bound in a solvent-exposed cleft, allowing facile replacement. We suggest a novel role for the conserved serine/threonine residue of the catalytic triad of SDR enzymes.


==About this Structure==
==About this Structure==
1KC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with MG, NDP and TRH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_reductase dTDP-4-dehydrorhamnose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.133 1.1.1.133] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KC3 OCA].  
1KC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NDP:'>NDP</scene> and <scene name='pdbligand=TRH:'>TRH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_reductase dTDP-4-dehydrorhamnose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.133 1.1.1.133] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KC3 OCA].  


==Reference==
==Reference==
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[[Category: dTDP-4-dehydrorhamnose reductase]]
[[Category: dTDP-4-dehydrorhamnose reductase]]
[[Category: Blankenfeldt, W.]]
[[Category: Blankenfeldt, W.]]
[[Category: Giraud, M.F.]]
[[Category: Giraud, M F.]]
[[Category: Graninger, M.]]
[[Category: Graninger, M.]]
[[Category: Kerr, I.D.]]
[[Category: Kerr, I D.]]
[[Category: Leonard, G.A.]]
[[Category: Leonard, G A.]]
[[Category: McMiken, H.J.]]
[[Category: McMiken, H J.]]
[[Category: Messner, P.]]
[[Category: Messner, P.]]
[[Category: Naismith, J.H.]]
[[Category: Naismith, J H.]]
[[Category: Whitfield, C.]]
[[Category: Whitfield, C.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: sugar-nucleotide-binding domain]]
[[Category: sugar-nucleotide-binding domain]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:02:47 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:26 2008''