2plc
|
PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C FROM LISTERIA MONOCYTOGENES
OverviewOverview
The X-ray crystal structure of the phosphatidylinositol-specific, phospholipase C (PI-PLC) from the human pathogen Listeria monocytogenes, has been determined both in free form at 2.0 A resolution, and in complex, with the competitive inhibitor myo-inositol at 2.6 A resolution. The, structure was solved by a combination of molecular replacement using the, structure of Bacillus cereus PI-PLC and single isomorphous replacement., The enzyme consists of a single (beta alpha)8-barrel domain with the, active site located at the C-terminal side of the beta-barrel. Unlike, other (beta alpha)8-barrels, the barrel in PI-PLC is open because it lacks, hydrogen bonding interactions between beta-strands V and VI. myo-Inositol, binds to the active site pocket by making specific hydrogen bonding, ... [(full description)]
About this StructureAbout this Structure
2PLC is a [Single protein] structure of sequence from [Listeria monocytogenes]. Active as [[1]], with EC number [3.1.4.10]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes., Moser J, Gerstel B, Meyer JE, Chakraborty T, Wehland J, Heinz DW, J Mol Biol. 1997 Oct 17;273(1):269-82. PMID:9367761
Page seeded by OCA on Mon Oct 29 16:10:01 2007