1qmd
From Proteopedia
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| - | [[Image:1qmd.jpg|left|200px]] | + | [[Image:1qmd.jpg|left|200px]] |
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| - | '''CALCIUM BOUND CLOSED FORM ALPHA-TOXIN FROM CLOSTRIDIUM PERFRINGENS''' | + | {{Structure |
| + | |PDB= 1qmd |SIZE=350|CAPTION= <scene name='initialview01'>1qmd</scene>, resolution 2.20Å | ||
| + | |SITE= <scene name='pdbsite=CA1:C-Terminal+Ca+(Membrane+Interactions).+In'>CA1</scene>, <scene name='pdbsite=CA2:C-Terminal+Ca+(Membrane+Interactions).+In'>CA2</scene>, <scene name='pdbsite=CA3:C-Terminal+Ca+(Membrane+Interactions).+In'>CA3</scene>, <scene name='pdbsite=CA4:C-Terminal+Ca+(Membrane+Interactions).+In'>CA4</scene>, <scene name='pdbsite=CA5:C-Terminal+Ca+(Membrane+Interactions).+In'>CA5</scene>, <scene name='pdbsite=CA6:C-Terminal+Ca+(Membrane+Interactions).+In'>CA6</scene>, <scene name='pdbsite=ZN1:Active+Site+Zn.+In+A+Molecule'>ZN1</scene>, <scene name='pdbsite=ZN2:Active+Site+Zn.+In+A+Molecule'>ZN2</scene>, <scene name='pdbsite=ZN3:Active+Site+Zn.+In+B+Molecule'>ZN3</scene> and <scene name='pdbsite=ZN4:Active+Site+Zn.+In+B+Molecule'>ZN4</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CALCIUM BOUND CLOSED FORM ALPHA-TOXIN FROM CLOSTRIDIUM PERFRINGENS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QMD is a [ | + | 1QMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMD OCA]. |
==Reference== | ==Reference== | ||
| - | Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin., Naylor CE, Jepson M, Crane DT, Titball RW, Miller J, Basak AK, Bolgiano B, J Mol Biol. 1999 Dec 3;294(3):757-70. PMID:[http:// | + | Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin., Naylor CE, Jepson M, Crane DT, Titball RW, Miller J, Basak AK, Bolgiano B, J Mol Biol. 1999 Dec 3;294(3):757-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10610794 10610794] |
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Phospholipase C]] | [[Category: Phospholipase C]] | ||
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[[Category: zinc phospholipase c]] | [[Category: zinc phospholipase c]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:42 2008'' |
Revision as of 11:39, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Sites: | , , , , , , , , and | ||||||
| Ligands: | and | ||||||
| Activity: | Phospholipase C, with EC number 3.1.4.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CALCIUM BOUND CLOSED FORM ALPHA-TOXIN FROM CLOSTRIDIUM PERFRINGENS
Overview
Alpha-toxin is the key determinant in gas-gangrene. The toxin, a phospholipase C, cleaves phosphatidylcholine in eukaryotic cell membranes. Calcium ions have been shown to be required for the specific binding of toxin to membranes prior to phospholipid cleavage. Reported X-ray crystallographic structures of the toxin show that the C-terminal domain has a fold that is analogous to the eukaryotic calcium and membrane-binding C2 domains. We report the binding sites for three calcium ions that have been identified, by crystallographic methods, in the C-terminal domain of the protein close to the postulated membrane-binding surface. The position of these ions at the tip of the domain, and their function (to facilitate membrane binding) is similar to that of calcium ions observed bound to C2 domains. Using the optical spectroscopic techniques of circular dichroism (CD) and fluorescence spectroscopy, pronounced changes to both near and far-UV CD and tryptophan emission fluorescence upon addition of calcium to the C-terminal domain of alpha-toxin have been observed. The changes in near-UV CD, fluorescence enhancement and a 2 nm blue-shift in the fluorescence emission spectrum are consistent with tryptophan residue(s) becoming more immobilised in a hydrophobic environment. Calcium binding appears to be low-affinity: Kd approximately 175-250 microM at pH 8 assuming a 1:1 stoichiometry. as measured by spectroscopic methods.
About this Structure
1QMD is a Single protein structure of sequence from Clostridium perfringens. Full crystallographic information is available from OCA.
Reference
Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin., Naylor CE, Jepson M, Crane DT, Titball RW, Miller J, Basak AK, Bolgiano B, J Mol Biol. 1999 Dec 3;294(3):757-70. PMID:10610794
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