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| {{STRUCTURE_1kp4| PDB=1kp4 | SCENE= }} | | {{STRUCTURE_1kp4| PDB=1kp4 | SCENE= }} |
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| '''CALCIUM-BOUND FORM OF PROKARYOTIC PHOSPHOLIPASE A2'''
| | ===CALCIUM-BOUND FORM OF PROKARYOTIC PHOSPHOLIPASE A2=== |
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| ==Overview==
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| 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).
| | The line below this paragraph, {{ABSTRACT_PUBMED_11897785}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11897785 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11897785}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Phospholipase a2]] | | [[Category: Phospholipase a2]] |
| [[Category: Prokaryote]] | | [[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 Wed Jul 2 10:41:28 2008'' |