1L5H

FeMo-cofactor Deficient Nitrogenase MoFe Protein

Summary for 1L5H

• Entry DOI: 10.2210/pdb1l5h/pdb
• Descriptor: nitrogenase molybdenum-iron protein alpha chain, nitrogenase molybdenum-iron protein beta chain, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: apo-protein, oxidoreductase
• Biological source: Azotobacter vinelandii; More
• Total number of polymer chains: 2
• Total formula weight: 115347.82

Authors

Schmid, B.,Ribbe, M.W.,Einsle, O.,Yoshida, M.,Thomas, L.M.,Dean, D.R.,Rees, D.C.,Burgess, B.K. (deposition date: 2002-03-06, release date: 2002-04-17, Last modification date: 2023-08-16)

Primary citation

Schmid, B.,Ribbe, M.W.,Einsle, O.,Yoshida, M.,Thomas, L.M.,Dean, D.R.,Rees, D.C.,Burgess, B.K.
Structure of a cofactor-deficient nitrogenase MoFe protein.
Science, 296:352-356, 2002

PubMed Abstract: 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 alpha and beta subunits. In this structure, one of the three alpha 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.

PubMed: 11951047
DOI: 10.1126/science.1070010

Experimental method

X-RAY DIFFRACTION (2.3 Å)