1p6d: Difference between revisions

Revision as of 05:05, 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:1p6d.png

Template:STRUCTURE 1p6d

STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH (3S)-3,4,DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINESTRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH (3S)-3,4,DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE

Template:ABSTRACT PUBMED 12921783

About this StructureAbout this Structure

1P6D is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

ReferenceReference

Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base., Antikainen NM, Monzingo AF, Franklin CL, Robertus JD, Martin SF, Arch Biochem Biophys. 2003 Sep 1;417(1):81-6. PMID:12921783

Page seeded by OCA on Mon Jul 28 05:05:11 2008

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OCA

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-[[Image:1p6d.jpg|left|200px]]
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 {{STRUCTURE_1p6d|  PDB=1p6d  |  SCENE=  }}
-'''STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH (3S)-3,4,DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE'''
+===STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH (3S)-3,4,DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE===
-==Overview==
+<!--
-Because mutations of the ionizable Asp at position 55 of the phosphatidylcholine preferring phospholipase C from Bacillus cereus (PLC(Bc)) to a non-ionizable Asn generate a mutant enzyme (D55N) with 10(4)-fold lower catalytic activity than the wild-type enzyme, we tentatively identified Asp55 as the general base for the enzymatic reaction. To eliminate the alternate possibility that Asp55 is a structurally important amino acid, the X-ray structures of unbound D55N and complexes of D55N with two non-hydrolyzable substrate analogues have been solved and refined to 2.0, 2.0, and 2.3A, respectively. The structures of unbound wild-type PLC(Bc) and a wild-type PLC(Bc)-complex with a non-hydrolyzable substrate analogue do not change significantly as a result of replacing Asp55 with Asn. These observations demonstrate that Asp55 is not critical for the structural integrity of the enzyme and support the hypothesis that Asp55 is the general base in the PLC(Bc)-catalyzed hydrolysis of phospholipids.
+The line below this paragraph, {{ABSTRACT_PUBMED_12921783}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12921783 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12921783}}
 ==About this Structure==
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 [[Category: Robertus, J D.]]
 [[Category: Tri zn2+ metal core]]
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