1cnf

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[[Image:1cnf.jpg|left|200px]]
[[Image:1cnf.jpg|left|200px]]
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{{Structure
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|PDB= 1cnf |SIZE=350|CAPTION= <scene name='initialview01'>1cnf</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1cnf", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrate_reductase_(NADH) Nitrate reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.1 1.7.1.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1cnf| PDB=1cnf | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnf OCA], [http://www.ebi.ac.uk/pdbsum/1cnf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cnf RCSB]</span>
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}}
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'''STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN'''
'''STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN'''
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==Reference==
==Reference==
Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain., Lu G, Lindqvist Y, Schneider G, Dwivedi U, Campbell W, J Mol Biol. 1995 May 19;248(5):931-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7760334 7760334]
Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain., Lu G, Lindqvist Y, Schneider G, Dwivedi U, Campbell W, J Mol Biol. 1995 May 19;248(5):931-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7760334 7760334]
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[[Category: Nitrate reductase (NADH)]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Zea mays]]
[[Category: Zea mays]]
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[[Category: Lu, G.]]
[[Category: Lu, G.]]
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
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[[Category: oxidoreductase (nitrogenous acceptor)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:55:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:54 2008''
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Revision as of 09:55, 2 May 2008

Template:STRUCTURE 1cnf

STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN


Overview

The refined crystal structures of the recombinant cytochrome b reductase fragment of corn (Zea mays) nitrate reductase, its ADP complex and the active-site mutant Cys242Ser are reported here. The native structure has been refined at 2.5 A resolution to a crystallographic R-factor of 18.7% with root-mean-square (r.m.s) deviations from standard bond lengths and angles of 0.013 A and 2.0 degrees. The diffraction pattern of the crystals is highly anisotropic and correction of this effect lowered the crystallographic R-factor by 5% during the refinement. The structure of the enzyme co-crystallized with ADP has been solved at 2.7 A resolution and refined to an R-factor of 18.6% with r.m.s. deviations from standard bond lengths and angles of 0.014 A and 2.1 degrees. It revealed the binding site of the ADP moiety of the NADH cofactor, which is the electron donor for nitrate reduction. Based on this structure, a model of NADH at the active site of the enzyme was built and the implications for electron transfer from NADH to the flavin cofactor are discussed. The crystal structure of an active-site mutant enzyme, Cys242Ser, has been solved by difference Fourier synthesis and refined to an R-factor of 19.0% to 3.0 A resolution with standard deviations of bond lengths and angles of 0.017 A and 2.5 degrees. This structure analysis suggests that the observed decrease in catalytic activity of this mutant might be due to misalignment of the nicotinamide ring in its binding site. A model of the heme-containing domain of nitrate reductase has been built based on the X-ray structure of bovine cytochrome b5 and has been docked with the cytochrome b reductase fragment of nitrate reductase. The model of the complex contains six salt-bridges at the domain-domain interface and a hydrophobic core. In this model, His48, an invariant residue in the cytochrome b reductase family, forms an interaction with the propionic acid group of the D-ring of the heme cofactor. This group is in contact with the C-8 methyl group of the flavin ring. Residues that might influence the redox potential of the flavin cofactor are proposed and their possible role in electron transfer is discussed.

About this Structure

1CNF is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain., Lu G, Lindqvist Y, Schneider G, Dwivedi U, Campbell W, J Mol Biol. 1995 May 19;248(5):931-48. PMID:7760334 Page seeded by OCA on Fri May 2 12:55:02 2008

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