2c8v

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spinqualitylabelsall models 2c8v, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

INSIGHTS INTO THE ROLE OF NUCLEOTIDE-DEPENDENT CONFORMATIONAL CHANGE IN NITROGENASE CATALYSIS: STRUCTURAL CHARACTERIZATION OF THE NITROGENASE FE PROTEIN LEU127 DELETION VARIANT WITH BOUND MGATP

Overview

In the present work, determination of the structure of the nitrogenase Leu, 127 deletion variant Fe protein with MgATP bound is presented, along with, density functional theory calculations, to provide insights into the roles, of MgATP in the nitrogenase reaction mechanism. Comparison of the, MgATP-bound structure of this Fe protein to the nucleotide-free form, indicates that the binding of MgATP does not alter the overall structure, of the variant significantly with only small differences in the, conformation of amino acids in direct contact with the two bound MgATP, molecules being seen. The earlier observation of splitting of the [4Fe-4S], cluster into two [2Fe-2S] clusters was observed to be unaltered upon, binding MgATP. Density functional theory was used to probe the assignment, of ligands to the two [2Fe-2S] rhombs. The Mg(2+) environment in the, MgATP-bound structure of the Leu127 deletion Fe protein is similar to that, observed for the Fe protein in the nitrogenase Fe protein: MoFe protein, complex stabilized by MgADP and tetrafluoroaluminate suggesting that large, scale conformational change implicated for the Fe protein may not be, mediated by changes in the Mg(2+) coordination. The results presented here, indicated that MgATP may enhance the stability of an open conformation and, prohibit intersubunit interactions, which have been implicated in, promoting nucleotide hydrolysis. This could be critical to the tight, control of MgATP hydrolysis observed within the nitrogenase complex and, may be important for maintaining unidirectional electron flow toward, substrate reduction.

About this Structure

2C8V is a Single protein structure of sequence from Azotobacter vinelandii with , and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Insights into the role of nucleotide-dependent conformational change in nitrogenase catalysis: Structural characterization of the nitrogenase Fe protein Leu127 deletion variant with bound MgATP., Sen S, Krishnakumar A, McClead J, Johnson MK, Seefeldt LC, Szilagyi RK, Peters JW, J Inorg Biochem. 2006 May;100(5-6):1041-52. Epub 2006 Mar 3. PMID:16616373

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