1kc3: Difference between revisions

Revision as of 10:06, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kc3.png

Template:STRUCTURE 1kc3

Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnoseCrystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose

Template:ABSTRACT PUBMED 12057193

About this StructureAbout this Structure

1KC3 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 10:06:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kc3.jpg|left|200px]]
+{{Seed}}
+[[Image:1kc3.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1kc3|  PDB=1kc3  |  SCENE=  }}
-'''Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose'''
+===Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12057193}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12057193 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12057193}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Rossman-fold]]
 [[Category: Sugar-nucleotide-binding domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:33:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:06:36 2008''