1hh8
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THE ACTIVE N-TERMINAL REGION OF P67PHOX: STRUCTURE AT 1.8 ANGSTROM RESOLUTION AND BIOCHEMICAL CHARACTERIZATIONS OF THE A128V MUTANT IMPLICATED IN CHRONIC GRANULOMATOUS DISEASE
OverviewOverview
Upon activation, the NADPH oxidase from neutrophils produces superoxide, anions in response to microbial infection. This enzymatic complex is, activated by association of its cytosolic factors p67(phox), p47(phox), and the small G protein Rac with a membrane-associated flavocytochrome, b(558). Here we report the crystal structure of the active N-terminal, fragment of p67(phox) at 1.8 A resolution, as well as functional studies, of p67(phox) mutants. This N-terminal region (residues 1-213) consists, mainly of four TPR (tetratricopeptide repeat) motifs in which the C, terminus folds back into a hydrophobic groove formed by the TPR domain., The structure is very similar to that of the inactive truncated form of, p67(phox) bound to the small G protein Rac previously reported, but, differs by ... [(full description)]
About this StructureAbout this Structure
1HH8 is a [Single protein] structure of sequence from [Homo sapiens] with FLC as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
The active N-terminal region of p67phox. Structure at 1.8 A resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease., Grizot S, Fieschi F, Dagher MC, Pebay-Peyroula E, J Biol Chem. 2001 Jun 15;276(24):21627-31. Epub 2001 Mar 21. PMID:11262407
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