1n2s: Difference between revisions
New page: left|200px<br /><applet load="1n2s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n2s, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1n2s.jpg|left|200px]]<br /><applet load="1n2s" size=" | [[Image:1n2s.jpg|left|200px]]<br /><applet load="1n2s" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1n2s, resolution 2.00Å" /> | caption="1n2s, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF DTDP-6-DEOXY-L-LYXO-4-HEXULOSE REDUCTASE (RMLD) IN COMPLEX WITH NADH'''<br /> | '''CRYSTAL STRUCTURE OF DTDP-6-DEOXY-L-LYXO-4-HEXULOSE REDUCTASE (RMLD) IN COMPLEX WITH NADH'''<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== | ||
1N2S 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 MG, NAD and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | 1N2S 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=MG:'>MG</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1KC0. 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=1N2S 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 14:01:38 2008'' | ||
Revision as of 12:01, 21 February 2008
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CRYSTAL STRUCTURE OF DTDP-6-DEOXY-L-LYXO-4-HEXULOSE REDUCTASE (RMLD) IN COMPLEX WITH NADH
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
1N2S is a Single protein structure of sequence from Salmonella enterica subsp. enterica serovar typhimurium with MG, NAD and TRS as ligands. This structure supersedes the now removed PDB entry 1KC0. 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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