1d2n

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(New page: 200px<br /> <applet load="1d2n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d2n, resolution 1.75&Aring;" /> '''D2 DOMAIN OF N-ETHY...)
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Revision as of 06:51, 18 November 2007

Image:1d2n.gif

1d2n, resolution 1.75Å

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D2 DOMAIN OF N-ETHYLMALEIMIDE-SENSITIVE FUSION PROTEIN

Overview

N-ethylmaleimide-sensitive fusion protein (NSF) is a cytosolic ATPase, required for many intracellular vesicle fusion reactions. NSF consists of, an amino-terminal region that interacts with other components of the, vesicle trafficking machinery, followed by two homologous ATP-binding, cassettes, designated D1 and D2, that possess essential ATPase and, hexamerization activities, respectively. The crystal structure of D2 bound, to Mg2+-AMPPNP has been determined at 1.75 A resolution. The structure, consists of a nucleotide-binding and a helical domain, and it is, unexpectedly similar to the first two domains of the clamp-loading subunit, delta' of E. coli DNA polymerase III. The structure suggests several, regions responsible for coupling of ATP hydrolysis to structural changes, in full-length NSF.

About this Structure

1D2N is a Single protein structure of sequence from Cricetulus griseus with MG, ANP and GOL as ligands. The following page contains interesting information on the relation of 1D2N with [AAA+ Proteases]. Full crystallographic information is available from OCA.

Reference

Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein., Lenzen CU, Steinmann D, Whiteheart SW, Weis WI, Cell. 1998 Aug 21;94(4):525-36. PMID:9727495

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