1kqd: Difference between revisions

Revision as of 10:46, 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:1kqd.png

Template:STRUCTURE 1kqd

Structure of Nitroreductase from E. cloacae Bound with 2e-Reduced Flavin Mononucleotide (FMN)Structure of Nitroreductase from E. cloacae Bound with 2e-Reduced Flavin Mononucleotide (FMN)

Template:ABSTRACT PUBMED 11805110

About this StructureAbout this Structure

1KQD is a Single protein structure of sequence from Enterobacter cloacae. Full crystallographic information is available from OCA.

ReferenceReference

Structures of nitroreductase in three states: effects of inhibitor binding and reduction., Haynes CA, Koder RL, Miller AF, Rodgers DW, J Biol Chem. 2002 Mar 29;277(13):11513-20. Epub 2002 Jan 22. PMID:11805110

Page seeded by OCA on Wed Jul 2 10:46:00 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kqd.gif|left|200px]]
+{{Seed}}
+[[Image:1kqd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1kqd|  PDB=1kqd  |  SCENE=  }}
-'''Structure of Nitroreductase from E. cloacae Bound with 2e-Reduced Flavin Mononucleotide (FMN)'''
+===Structure of Nitroreductase from E. cloacae Bound with 2e-Reduced Flavin Mononucleotide (FMN)===
-==Overview==
+<!--
-The crystal structure of the nitroreductase enzyme from Enterobacter cloacae has been determined for the oxidized form in separate complexes with benzoate and acetate inhibitors and for the two-electron reduced form. Nitroreductase is a member of a group of enzymes that reduce a broad range of nitroaromatic compounds and has potential uses in chemotherapy and bioremediation. The monomers of the nitroreductase dimer adopt an alpha+beta fold and together bind two flavin mononucleotide prosthetic groups at the dimer interface. In the oxidized enzyme, the flavin ring system adopts a strongly bent (16 degrees ) conformation, and the bend increases (25 degrees ) in the reduced form of the enzyme, roughly the conformation predicted for reduced flavin free in solution. Because free oxidized flavin is planar, the induced bend in the oxidized enzyme may favor reduction, and it may also account for the characteristic inability of the enzyme to stabilize the one electron-reduced semiquinone flavin, which is also planar. Both inhibitors bind over the pyrimidine and central rings of the flavin in partially overlapping sites. Comparison of the two inhibitor complexes shows that a portion of helix H6 can flex to accommodate the differently sized inhibitors suggesting a mechanism for accommodating varied substrates.
+The line below this paragraph, {{ABSTRACT_PUBMED_11805110}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11805110 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11805110}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Nitroreductase]]
 [[Category: Reduced hydroquinone]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:02:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:46:00 2008''