2plc: Difference between revisions
New page: left|200px<br /> <applet load="2plc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2plc, resolution 2.0Å" /> '''PHOSPHATIDYLINOSITOL... |
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==About this Structure== | ==About this Structure== | ||
2PLC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.10 3.1.4.10]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PLC OCA]]. | 2PLC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.10 3.1.4.10]]. Structure known Active Site: CIC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PLC OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: virulence factor of human pathogen]] | [[Category: virulence factor of human pathogen]] | ||
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Revision as of 09:25, 30 October 2007
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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 [Hydrolase], with EC number [3.1.4.10]. Structure known Active Site: CIC. 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
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