1poc: Difference between revisions
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==CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE== | ==CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE== | ||
<StructureSection load='1poc' size='340' side='right' caption='[[1poc]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1poc' size='340' side='right'caption='[[1poc]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1poc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apime Apime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1POC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1poc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apime Apime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1POC FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1poc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1poc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Phospholipase A2|Phospholipase A2]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Apime]] | [[Category: Apime]] | ||
[[Category: Large Structures]] | |||
[[Category: Otwinowski, Z]] | [[Category: Otwinowski, Z]] | ||
[[Category: Scott, D L]] | [[Category: Scott, D L]] | ||
[[Category: Sigler, P B]] | [[Category: Sigler, P B]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 13:59, 17 July 2019
CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUECRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE
Structural highlights
Function[PA2_APIME] PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism. Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue.,Scott DL, Otwinowski Z, Gelb MH, Sigler PB Science. 1990 Dec 14;250(4987):1563-6. PMID:2274788[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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