1kp4
From Proteopedia
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'''CALCIUM-BOUND FORM OF PROKARYOTIC PHOSPHOLIPASE A2''' | '''CALCIUM-BOUND FORM OF PROKARYOTIC PHOSPHOLIPASE A2''' | ||
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==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11897785 11897785] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11897785 11897785] | ||
| - | [[Category: Phospholipase A(2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces violaceoruber]] | [[Category: Streptomyces violaceoruber]] | ||
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[[Category: Matoba, Y.]] | [[Category: Matoba, Y.]] | ||
[[Category: Sugiyama, M.]] | [[Category: Sugiyama, M.]] | ||
| - | [[Category: | + | [[Category: Calcium ion]] |
| - | [[Category: | + | [[Category: Phospholipase a2]] |
| - | [[Category: | + | [[Category: Prokaryote]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:00:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:00, 2 May 2008
CALCIUM-BOUND FORM 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
1KP4 is a Single protein structure of sequence from Streptomyces violaceoruber. 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 Fri May 2 23:00:14 2008
