1faz
From Proteopedia
(New page: 200px<br /><applet load="1faz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1faz, resolution 1.40Å" /> '''THE CRYSTAL STRUCTUR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1faz.gif|left|200px]]<br /><applet load="1faz" size=" | + | [[Image:1faz.gif|left|200px]]<br /><applet load="1faz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1faz, resolution 1.40Å" /> | caption="1faz, resolution 1.40Å" /> | ||
'''THE CRYSTAL STRUCTURE OF PROKARYOTIC PHOSPHOLIPASE A2'''<br /> | '''THE CRYSTAL STRUCTURE OF PROKARYOTIC PHOSPHOLIPASE A2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In this study, the x-ray crystal structures of the calcium-free and | + | In this study, the x-ray crystal structures of the calcium-free and calcium-bound forms of phospholipase A(2) (PLA(2)), produced extracellularly by Streptomyces violaceoruber, were determined by using the multiple isomorphous replacement and molecular replacement methods, respectively. The former and latter structures were refined to an R-factor of 18.8% at a 1.4-A resolution and an R-factor of 15.0% at a 1.6-A resolution, respectively. The overall structure of the prokaryotic PLA(2) exhibits a novel folding topology that demonstrates that it is completely distinct from those of eukaryotic PLA(2)s, which have been already determined by x-ray and NMR analyses. Furthermore, the coordination geometry of the calcium(II) ion apparently deviated from that of eukaryotic PLA(2)s. Regardless of the evolutionary divergence, the catalytic mechanism including the calcium(II) ion on secreted PLA(2) seems to be conserved between prokaryotic and eukaryotic cells. Demonstrating that the overall structure determined by x-ray analysis is almost the same as that determined by NMR analysis is useful to discuss the catalytic mechanism at the molecular level of the bacterial PLA(2). |
==About this Structure== | ==About this Structure== | ||
| - | 1FAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber]. 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:// | + | 1FAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber]. 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=1FAZ OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: streptomyces violaceoruber]] | [[Category: streptomyces violaceoruber]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:44 2008'' |
Revision as of 10:36, 21 February 2008
|
THE CRYSTAL STRUCTURE OF PROKARYOTIC PHOSPHOLIPASE A2
Overview
In this study, the x-ray crystal structures of the calcium-free and calcium-bound forms of phospholipase A(2) (PLA(2)), produced extracellularly by Streptomyces violaceoruber, were determined by using the multiple isomorphous replacement and molecular replacement methods, respectively. The former and latter structures were refined to an R-factor of 18.8% at a 1.4-A resolution and an R-factor of 15.0% at a 1.6-A resolution, respectively. The overall structure of the prokaryotic PLA(2) exhibits a novel folding topology that demonstrates that it is completely distinct from those of eukaryotic PLA(2)s, which have been already determined by x-ray and NMR analyses. Furthermore, the coordination geometry of the calcium(II) ion apparently deviated from that of eukaryotic PLA(2)s. Regardless of the evolutionary divergence, the catalytic mechanism including the calcium(II) ion on secreted PLA(2) seems to be conserved between prokaryotic and eukaryotic cells. Demonstrating that the overall structure determined by x-ray analysis is almost the same as that determined by NMR analysis is useful to discuss the catalytic mechanism at the molecular level of the bacterial PLA(2).
About this Structure
1FAZ is a Single protein structure of sequence from Streptomyces violaceoruber. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
The crystal structure of prokaryotic phospholipase A2., Matoba Y, Katsube Y, Sugiyama M, J Biol Chem. 2002 May 31;277(22):20059-69. Epub 2002 Mar 15. PMID:11897785
Page seeded by OCA on Thu Feb 21 12:36:44 2008
