3p2p

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(New page: 200px<br /><applet load="3p2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="3p2p, resolution 2.1&Aring;" /> '''ENHANCED ACTIVITY AND...)
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[[Image:3p2p.jpg|left|200px]]<br /><applet load="3p2p" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:3p2p.jpg|left|200px]]<br /><applet load="3p2p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3p2p, resolution 2.1&Aring;" />
caption="3p2p, resolution 2.1&Aring;" />
'''ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP'''<br />
'''ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP'''<br />
==Overview==
==Overview==
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Protein engineering and x-ray crystallography have been used to study the, role of a surface loop that is present in pancreatic phospholipases but is, absent in snake venom phospholipases. Removal of residues 62 to 66 from, porcine pancreatic phospholipase A2 does not change the binding constant, for micelles significantly, but it improves catalytic activity up to 16, times on micellar (zwitterionic) lecithin substrates. In contrast, the, decrease in activity on negatively charged substrates is greater than, fourfold. A crystallographic study of the mutant enzyme shows that the, region of the deletion has a well-defined structure that differs from the, structure of the wild-type enzyme. No structural changes in the active, site of the enzyme were detected.
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Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.
==About this Structure==
==About this Structure==
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3P2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] 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=3P2P OCA].
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3P2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] 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=3P2P OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra, B W.]]
[[Category: Drenth, J.]]
[[Category: Drenth, J.]]
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[[Category: Kalk, K.H.]]
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[[Category: Kalk, K H.]]
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[[Category: Thunnissen, M.M.G.M.]]
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[[Category: Thunnissen, M M.G M.]]
[[Category: CA]]
[[Category: CA]]
[[Category: hydrolase(carboxyl ester)]]
[[Category: hydrolase(carboxyl ester)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:54:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:36 2008''

Revision as of 17:10, 21 February 2008


3p2p, resolution 2.1Å

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ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP

Overview

Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.

About this Structure

3P2P is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop., Kuipers OP, Thunnissen MM, de Geus P, Dijkstra BW, Drenth J, Verheij HM, de Haas GH, Science. 1989 Apr 7;244(4900):82-5. PMID:2704992

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