This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kbz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1kbz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kbz, resolution 2.20&Aring;" /> '''Crystal Structure of...)
Line 1: Line 1:
-
[[Image:1kbz.jpg|left|200px]]<br /><applet load="1kbz" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1kbz.jpg|left|200px]]<br /><applet load="1kbz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kbz, resolution 2.20&Aring;" />
caption="1kbz, resolution 2.20&Aring;" />
'''Crystal Structure of apo-dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) from Salmonella enterica serovar Typhimurium'''<br />
'''Crystal Structure of apo-dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) from Salmonella enterica serovar Typhimurium'''<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==
-
1KBZ 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1KBZ OCA].
+
1KBZ 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1KBZ OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[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]]
Line 27: Line 27:
[[Category: sugar-nucleotide-binding domain]]
[[Category: sugar-nucleotide-binding domain]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:02:32 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:25 2008''

Revision as of 11:32, 21 February 2008


1kbz, resolution 2.20Å

Drag the structure with the mouse to rotate

Crystal Structure of apo-dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) from Salmonella enterica serovar Typhimurium

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

1KBZ is a Single protein structure of sequence from Salmonella typhimurium with as ligand. 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

Page seeded by OCA on Thu Feb 21 13:32:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools