2c8v

From Proteopedia

Revision as of 12:17, 30 October 2007

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 ... [(full description)]

About this Structure

2C8V is a [Single protein] structure of sequence from [Azotobacter vinelandii] with MG, FS1 and ATP as [ligands]. Active as [Nitrogenase], with EC number [1.18.6.1]. Structure known Active Site: AC1. 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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