1drv
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(New page: 200px<br /> <applet load="1drv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1drv, resolution 2.2Å" /> '''ESCHERICHIA COLI DHP...)
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Revision as of 17:50, 29 October 2007
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ESCHERICHIA COLI DHPR/ACNADH COMPLEX
Overview
E. coli dihydrodipicolinate reductase exhibits unusual nucleotide, specificity, with NADH being kinetically twice as effective as NADPH as a, reductant as evidenced by their relative V/K values. To investigate the, nature of the interactions which determine this specificity, we performed, isothermal titration calorimetry to determine the thermodynamic parameters, of binding and determined the three-dimensional structures of the, corresponding enzyme-nucleotide complexes. The thermodynamic binding, parameters for NADPH and NADH were determined to be Kd = 2.12 microM, delta G degree = -7.81 kcal mol-1, delta H degree = -10.98 kcal mol-1, and, delta S degree = -10.5 cal mol-1 deg-1 and Kd = 0.46 microM, delta G, degree = -8.74 kcal mol-1, delta H degree = -8.93 kcal mol-1, and delta S, ... [(full description)]
About this Structure
1DRV is a [Single protein] structure of sequence from [Escherichia coli] with A3D as [ligand]. Active as [[1]], with EC number [1.3.1.26]. Full crystallographic information is available from [OCA].
Reference
Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes., Reddy SG, Scapin G, Blanchard JS, Biochemistry. 1996 Oct 15;35(41):13294-302. PMID:8873595
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