1olp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1olp. | [[Image:1olp.jpg|left|200px]]<br /><applet load="1olp" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1olp" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1olp, resolution 2.50Å" /> | caption="1olp, resolution 2.50Å" /> | ||
'''ALPHA TOXIN FROM CLOSTRIDIUM ABSONUM'''<br /> | '''ALPHA TOXIN FROM CLOSTRIDIUM ABSONUM'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
1OLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_sardiniense Clostridium sardiniense] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] | 1OLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_sardiniense Clostridium sardiniense] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Known structural/functional Site: <scene name='pdbsite=AC1:Zn Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OLP OCA]. | ||
==Reference== | ==Reference== | ||
| Line 25: | Line 24: | ||
[[Category: zinc phospholipase c]] | [[Category: zinc phospholipase c]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:49:40 2007'' | ||
Revision as of 18:39, 18 December 2007
|
ALPHA TOXIN FROM CLOSTRIDIUM ABSONUM
OverviewOverview
Clostridium absonum phospholipase C (Caa) is a 42.7 kDa protein, which, shows 60% amino acid sequence identity with the Clostridium perfringens, phospholipase C, or alpha-toxin (Cpa), and has been isolated from patients, suffering from gas gangrene. We report the cloning and sequencing, purification, characterisation and crystal structure of the Caa enzyme., Caa had twice the phospholipid-hydrolysing (lecithinase) activity, 1.5, times the haemolytic activity and over seven times the activity towards, phosphatidylcholine-based liposomes when compared with Cpa. However, the, Caa enzyme had a lower activity than Cpa to the free (i.e. not in lipid, bilayer) substrate para-nitrophenylphosphorylcholine, towards, sphingomyelin-based liposomes and showed half the cytotoxicity. The lethal, dose (LD(50)) of Caa in mice was approximately twice that of Cpa. The, crystal structure of Caa shows that the 72-93 residue loop is in a, conformation different from those of previously determined open-form, alpha-toxin structures. This conformational change suggests a role for W84, in membrane binding and a possible route of entry into the active site, along a hydrophobic channel created by the re-arrangement of this loop., Overall, the properties of Caa are compatible with a role as a, virulence-determinant in gas gangrene caused by C.absonum.
About this StructureAbout this Structure
1OLP is a Single protein structure of sequence from Clostridium sardiniense with CA and ZN as ligands. Active as Phospholipase C, with EC number 3.1.4.3 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Clostridium absonum alpha-toxin: new insights into clostridial phospholipase C substrate binding and specificity., Clark GC, Briggs DC, Karasawa T, Wang X, Cole AR, Maegawa T, Jayasekera PN, Naylor CE, Miller J, Moss DS, Nakamura S, Basak AK, Titball RW, J Mol Biol. 2003 Oct 31;333(4):759-69. PMID:14568535
Page seeded by OCA on Tue Dec 18 17:49:40 2007