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.
2or2
From Proteopedia
(New page: 200px<br /><applet load="2or2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2or2, resolution 1.840Å" /> '''Structure of the W4...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2or2.gif|left|200px]]<br /><applet load="2or2" size=" | + | [[Image:2or2.gif|left|200px]]<br /><applet load="2or2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2or2, resolution 1.840Å" /> | caption="2or2, resolution 1.840Å" /> | ||
'''Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C'''<br /> | '''Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2OR2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Active as [http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] Full crystallographic information is available from [http:// | + | 2OR2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Active as [http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OR2 OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 28: | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:04:26 2008'' |
Revision as of 13:04, 23 January 2008
|
Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C
Overview
The crystal structure of the W47/242A mutant of, phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus, thuringiensis has been solved to 1.8 A resolution. The W47/242A mutant is, an interfacially-challenged enzyme, and it has been proposed that one or, both tryptophan side chains serve as membrane interfacial anchors (Feng et, al. (2002) J. Biol. Chem. 277, 19867-75). The crystal structure supports, this hypothesis. Relative to the crystal structure of the closely-related, (97% identity) wild-type PI-PLC from B. cereus, significant conformational, differences occur at the membrane-binding interfacial region rather than, the active site. The TrpAla mutations not only remove the, membrane-partitioning aromatic side chains but also perturb the, conformations of the so-called helix B and rim loop regions, both of which, are implicated in interfacial binding. The crystal structure also reveals, a homodimer, the first such observation for a bacterial PI-PLC, with, pseudo 2-fold symmetry. The symmetric dimer interface is stabilized by, hydrophobic and hydrogen-bonding interactions, contributed primarily by a, central swath of aromatic residues arranged in a quasi-herringbone, pattern. Evidence that interfacially-active wild-type PI-PLC enzymes may, dimerize in the presence of phosphatidylcholine vesicles is provided by, fluorescence quenching of PI-PLC mutants with pyrene-labeled cysteine, residues. The combined data suggest that wild-type PI-PLC can form similar, homodimers, anchored to the interface by the tryptophan and neighboring, membrane-partitioning residues.
About this Structure
2OR2 is a Single protein structure of sequence from Bacillus thuringiensis. Active as Phosphatidylinositol diacylglycerol-lyase, with EC number 4.6.1.13 Full crystallographic information is available from OCA.
Reference
Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C., Shao C, Shi X, Wehbi H, Zambonelli C, Head JF, Seaton BA, Roberts MF, J Biol Chem. 2007 Jan 9;. PMID:17213187
Page seeded by OCA on Wed Jan 23 15:04:26 2008
Categories: Bacillus thuringiensis | Phosphatidylinositol diacylglycerol-lyase | Single protein | Head, J.F. | Roberts, M.F. | Seaton, B.A. | Shao, C. | Shi, X. | Wehbi, H. | Zambonelli, C. | Dimer | Interfacially impaired | Membrane binding | Phosphatidylinositol-specific phospholipase c | Pi-plc | Tim barrel
