1ptd: Difference between revisions

Revision as of 21:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ptd.png

Template:STRUCTURE 1ptd

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE CPHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C

Template:ABSTRACT PUBMED 7664726

About this StructureAbout this Structure

1PTD is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol., Heinz DW, Ryan M, Bullock TL, Griffith OH, EMBO J. 1995 Aug 15;14(16):3855-63. PMID:7664726

Page seeded by OCA on Mon Jul 28 21:21:58 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ptd.jpg|left|200px]]
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 {{STRUCTURE_1ptd|  PDB=1ptd  |  SCENE=  }}
-'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C'''
+===PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C===
-==Overview==
+<!--
-Phosphatidylinositol (PI), once regarded as an obscure component of membranes, is now recognized as an important reservoir of second messenger precursors and as an anchor for membrane enzymes. PI-specific phospholipase C (PI-PLC) is the enzyme that cleaves PI, invoking numerous cellular responses. The crystal structure of PI-PLC from Bacillus cereus (EC 3.1.4.10) has been solved at 2.6 A resolution and refined to a crystallographic R factor of 18.7%. The structure consists of an imperfect (beta alpha)8-barrel similar to that first observed for triose phosphate isomerase and does not resemble any other known phospholipase structure. The active site of the enzyme has been identified by determining the structure of PI-PLC in complex with its inhibitor, myo-inositol, at 2.6 A resolution (R factor = 19.5%). This substrate-like inhibitor interacts with a number of residues highly conserved among prokaryotic PI-PLCs. Residues His32 and His82, which are also conserved between prokaryotic and eukaryotic PI-PLCs, most likely act as general base and acid respectively in a catalytic mechanism analogous to that observed for ribonucleases.
+The line below this paragraph, {{ABSTRACT_PUBMED_7664726}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7664726 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7664726}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Phosphatidylinositol specific phospholipase c]]
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