Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inser...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2002-04, Vol.296 (5566), p.352-356
Main Authors: Schmid, Benedikt, Ribbe, Markus W., Einsle, Oliver, Yoshida, Mika, Thomas, Leonard M., Dean, Dennis R., Rees, Douglas C., Burgess, Barbara K.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Ammonia
Analytical, structural and metabolic biochemistry
Atoms
Azotobacter vinelandii - enzymology
Binding Sites
Biochemistry
Biological and medical sciences
Color semiotics
Crystallization
Crystallography
Crystallography, X-Ray
Dimerization
Enzymes
Enzymes and enzyme inhibitors
Evaluation
Fundamental and applied biological sciences. Psychology
Gene expression
Genetic research
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data
Molybdoferredoxin - chemistry
Molybdoferredoxin - genetics
Molybdoferredoxin - metabolism
Muscles
Nitrogenase
Oral poliovirus vaccine
Oxidoreductases
Poliomyelitis
Poliovirus
Protein Conformation
Protein Folding
Protein research
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Skeletal muscle
Static Electricity
Surface Properties
Transgenic animals
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous α and β subunits. In this structure, one of the three α subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1070010