1mc2

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(New page: 200px<br /><applet load="1mc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mc2, resolution 0.85&Aring;" /> '''monomeric LYS-49 pho...)
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[[Image:1mc2.gif|left|200px]]<br /><applet load="1mc2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mc2.gif|left|200px]]<br /><applet load="1mc2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mc2, resolution 0.85&Aring;" />
caption="1mc2, resolution 0.85&Aring;" />
'''monomeric LYS-49 phospholipase A2 homologue purified from AG'''<br />
'''monomeric LYS-49 phospholipase A2 homologue purified from AG'''<br />
==Overview==
==Overview==
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The crystal structure of acutohaemolysin, a lysine 49 phospholipase A2, protein with 1010 non-hydrogen protein atoms and 232 water molecules, has, been determined ab initio using the program SnB at an ultrahigh resolution, of 0.8 A. The lack of catalytic activity appears to be related to the, presence of Phe102, which prevents the access of substrate to the active, site. The substitution of tryptophan for leucine at residue 10 interferes, with dimer formation and may be responsible for the additional loss of, hemolytic activity. The ultrahigh resolution of the experimental, diffraction data permits alternative conformations to be modeled for, disordered residues, many hydrogen atoms to be located, the protonation of, the Nepsilon2 atom in the catalytic residue His48 to be observed, experimentally, and the density of the bonding electrons to be analyzed in, detail.
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The crystal structure of acutohaemolysin, a lysine 49 phospholipase A2 protein with 1010 non-hydrogen protein atoms and 232 water molecules, has been determined ab initio using the program SnB at an ultrahigh resolution of 0.8 A. The lack of catalytic activity appears to be related to the presence of Phe102, which prevents the access of substrate to the active site. The substitution of tryptophan for leucine at residue 10 interferes with dimer formation and may be responsible for the additional loss of hemolytic activity. The ultrahigh resolution of the experimental diffraction data permits alternative conformations to be modeled for disordered residues, many hydrogen atoms to be located, the protonation of the Nepsilon2 atom in the catalytic residue His48 to be observed experimentally, and the density of the bonding electrons to be analyzed in detail.
==About this Structure==
==About this Structure==
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1MC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MC2 OCA].
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1MC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus] with <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MC2 OCA].
==Reference==
==Reference==
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[[Category: Deinagkistrodon acutus]]
[[Category: Deinagkistrodon acutus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Huang, Q.Q.]]
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[[Category: Huang, Q Q.]]
[[Category: Jelsch, C.]]
[[Category: Jelsch, C.]]
[[Category: Liu, Q.]]
[[Category: Liu, Q.]]
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[[Category: Niu, L.W.]]
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[[Category: Niu, L W.]]
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[[Category: Teng, M.K.]]
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[[Category: Teng, M K.]]
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[[Category: Weeks, C.M.]]
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[[Category: Weeks, C M.]]
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[[Category: Zhang, R.G.]]
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[[Category: Zhang, R G.]]
[[Category: IPA]]
[[Category: IPA]]
[[Category: agkistrodon acutus]]
[[Category: agkistrodon acutus]]
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[[Category: ys49-phospholipase a2]]
[[Category: ys49-phospholipase a2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:19:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:42 2008''

Revision as of 11:53, 21 February 2008


1mc2, resolution 0.85Å

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monomeric LYS-49 phospholipase A2 homologue purified from AG

Overview

The crystal structure of acutohaemolysin, a lysine 49 phospholipase A2 protein with 1010 non-hydrogen protein atoms and 232 water molecules, has been determined ab initio using the program SnB at an ultrahigh resolution of 0.8 A. The lack of catalytic activity appears to be related to the presence of Phe102, which prevents the access of substrate to the active site. The substitution of tryptophan for leucine at residue 10 interferes with dimer formation and may be responsible for the additional loss of hemolytic activity. The ultrahigh resolution of the experimental diffraction data permits alternative conformations to be modeled for disordered residues, many hydrogen atoms to be located, the protonation of the Nepsilon2 atom in the catalytic residue His48 to be observed experimentally, and the density of the bonding electrons to be analyzed in detail.

About this Structure

1MC2 is a Single protein structure of sequence from Deinagkistrodon acutus with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of a novel, inactive, lysine 49 PLA2 from Agkistrodon acutus venom: an ultrahigh resolution, AB initio structure determination., Liu Q, Huang Q, Teng M, Weeks CM, Jelsch C, Zhang R, Niu L, J Biol Chem. 2003 Oct 17;278(42):41400-8. Epub 2003 Jul 19. PMID:12871974

Page seeded by OCA on Thu Feb 21 13:53:42 2008

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