This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1p6e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p6e.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1p6e.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p6e| PDB=1p6e | SCENE= }}
{{STRUCTURE_1p6e| PDB=1p6e | SCENE= }}
-
'''STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE'''
+
===STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE===
-
==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==
==About this Structure==
Line 30: Line 34:
[[Category: Protein-phospholipid analogue complex]]
[[Category: Protein-phospholipid analogue complex]]
[[Category: Tri zn+2 metal core]]
[[Category: Tri zn+2 metal core]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:44:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:27:17 2008''

Revision as of 20:27, 28 July 2008

Image:1p6e.png

Template:STRUCTURE 1p6e

STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE

Template:ABSTRACT PUBMED 12921783

About this Structure

1P6E is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

Reference

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 23:27:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p6e"
Personal tools