1pc9
From Proteopedia
(New page: 200px<br /><applet load="1pc9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pc9, resolution 2.5Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1pc9.gif|left|200px]]<br /><applet load="1pc9" size=" | + | [[Image:1pc9.gif|left|200px]]<br /><applet load="1pc9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pc9, resolution 2.5Å" /> | caption="1pc9, resolution 2.5Å" /> | ||
'''Crystal Structure of BnSP-6, a Lys49-Phospholipase A2'''<br /> | '''Crystal Structure of BnSP-6, a Lys49-Phospholipase A2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phospholipases A(2) are components of Bothrops venoms responsible for | + | Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent. |
==About this Structure== | ==About this Structure== | ||
| - | 1PC9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bothrops_neuwiedi_pauloensis Bothrops neuwiedi pauloensis]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http:// | + | 1PC9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bothrops_neuwiedi_pauloensis Bothrops neuwiedi pauloensis]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phospholipase A(2)]] | [[Category: Phospholipase A(2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fontes, M | + | [[Category: Fontes, M R.M.]] |
| - | [[Category: Giglio, J | + | [[Category: Giglio, J R.]] |
| - | [[Category: Magro, A | + | [[Category: Magro, A J.]] |
| - | [[Category: Soares, A | + | [[Category: Soares, A M.]] |
[[Category: bothrops]] | [[Category: bothrops]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: venom.]] | [[Category: venom.]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:21 2008'' |
Revision as of 12:27, 21 February 2008
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Crystal Structure of BnSP-6, a Lys49-Phospholipase A2
Overview
Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent.
About this Structure
1PC9 is a Single protein structure of sequence from Bothrops neuwiedi pauloensis. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights., Magro AJ, Soares AM, Giglio JR, Fontes MR, Biochem Biophys Res Commun. 2003 Nov 21;311(3):713-20. PMID:14623331
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