1kp4: Difference between revisions

Revision as of 14:36, 21 February 2008

CALCIUM-BOUND FORM OF PROKARYOTIC PHOSPHOLIPASE A2

OverviewOverview

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 StructureAbout this Structure

1KP4 is a Single protein structure of sequence from Streptomyces violaceoruber with as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

ReferenceReference

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 13:36:30 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kp4.jpg|left|200px]]<br /><applet load="1kp4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kp4.jpg|left|200px]]<br /><applet load="1kp4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kp4, resolution 1.60&Aring;" />
 '''CALCIUM-BOUND FORM OF PROKARYOTIC PHOSPHOLIPASE A2'''<br />
 ==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).
+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==
-KP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KP4 OCA].
+KP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1KP4 OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: prokaryote]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:42:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:30 2008''