1kc1
From Proteopedia
(New page: 200px<br /><applet load="1kc1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kc1, resolution 2.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1kc1.jpg|left|200px]]<br /><applet load="1kc1" size=" | + | [[Image:1kc1.jpg|left|200px]]<br /><applet load="1kc1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kc1, resolution 2.60Å" /> | caption="1kc1, resolution 2.60Å" /> | ||
'''Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH'''<br /> | '''Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) catalyzes the final step | + | 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== | ||
| - | 1KC1 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, SO4 and NDP 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:// | + | 1KC1 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=SO4:'>SO4</scene> and <scene name='pdbligand=NDP:'>NDP</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=1KC1 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 | + | [[Category: Giraud, M F.]] |
[[Category: Graninger, M.]] | [[Category: Graninger, M.]] | ||
| - | [[Category: Kerr, I | + | [[Category: Kerr, I D.]] |
| - | [[Category: Leonard, G | + | [[Category: Leonard, G A.]] |
| - | [[Category: McMiken, H | + | [[Category: McMiken, H J.]] |
[[Category: Messner, P.]] | [[Category: Messner, P.]] | ||
| - | [[Category: Naismith, J | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:24 2008'' |
Revision as of 11:32, 21 February 2008
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Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH
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.
About this Structure
1KC1 is a Single protein structure of sequence from Salmonella typhimurium with , and as ligands. Active as dTDP-4-dehydrorhamnose reductase, with EC number 1.1.1.133 Full crystallographic information is available from OCA.
Reference
Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose reductase (RmlD) shows a new Mg2+-dependent dimerization mode., Blankenfeldt W, Kerr ID, Giraud MF, McMiken HJ, Leonard G, Whitfield C, Messner P, Graninger M, Naismith JH, Structure. 2002 Jun;10(6):773-86. PMID:12057193
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