1fb2: Difference between revisions

Revision as of 13:36, 21 February 2008

STRUCTURE OF PHOSPHOLIPASE A2 FROM DABOIA RUSSELLI PULCHELLA AT 1.95

OverviewOverview

The crystal structure of phospholipase A(2) from the venom of Daboia russelli pulchella has been refined to an R factor of 0.216 using 17,922 reflections to 1.9 A resolution. The structure contains two crystallographically independent molecules in the asymmetric unit. The overall conformations of the two molecules are essentially the same except for three regions, namely the calcium-binding loop including Trp31, the beta-wing and the C-terminal residues 119-131. Although these differences have apparently been caused by molecular packing, they seem to have functional relevance. Particularly noteworthy is the conformation of Trp31, which is favourable for substrate binding in one molecule as it is aligned with one of the side walls of the hydrophobic channel, whereas in the other molecule it is located at the mouth of the channel, thereby blocking the entry of substrates leading to loss of activity. This feature is unique to the present structure and does not occur in the dimers and trimers of other PLA(2)s.

About this StructureAbout this Structure

1FB2 is a Single protein structure of sequence from Daboia russellii pulchella. Full crystallographic information is available from OCA.

ReferenceReference

Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution., Chandra V, Kaur P, Jasti J, Betzel C, Singh TP, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1793-8. Epub 2001, Nov 21. PMID:11717491

Page seeded by OCA on Thu Feb 21 12:36:52 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1fb2.gif|left|200px]]<br /><applet load="1fb2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fb2.gif|left|200px]]<br /><applet load="1fb2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fb2, resolution 1.95&Aring;" />
 '''STRUCTURE OF PHOSPHOLIPASE A2 FROM DABOIA RUSSELLI PULCHELLA AT 1.95'''<br />
 ==Overview==
-The crystal structure of phospholipase A(2) from the venom of Daboia, russelli pulchella has been refined to an R factor of 0.216 using 17,922, reflections to 1.9 A resolution. The structure contains two, crystallographically independent molecules in the asymmetric unit. The, overall conformations of the two molecules are essentially the same except, for three regions, namely the calcium-binding loop including Trp31, the, beta-wing and the C-terminal residues 119-131. Although these differences, have apparently been caused by molecular packing, they seem to have, functional relevance. Particularly noteworthy is the conformation of, Trp31, which is favourable for substrate binding in one molecule as it is, aligned with one of the side walls of the hydrophobic channel, whereas in, the other molecule it is located at the mouth of the channel, thereby, blocking the entry of substrates leading to loss of activity. This feature, is unique to the present structure and does not occur in the dimers and, trimers of other PLA(2)s.
+The crystal structure of phospholipase A(2) from the venom of Daboia russelli pulchella has been refined to an R factor of 0.216 using 17,922 reflections to 1.9 A resolution. The structure contains two crystallographically independent molecules in the asymmetric unit. The overall conformations of the two molecules are essentially the same except for three regions, namely the calcium-binding loop including Trp31, the beta-wing and the C-terminal residues 119-131. Although these differences have apparently been caused by molecular packing, they seem to have functional relevance. Particularly noteworthy is the conformation of Trp31, which is favourable for substrate binding in one molecule as it is aligned with one of the side walls of the hydrophobic channel, whereas in the other molecule it is located at the mouth of the channel, thereby blocking the entry of substrates leading to loss of activity. This feature is unique to the present structure and does not occur in the dimers and trimers of other PLA(2)s.
 ==About this Structure==
-FB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_pulchella Daboia russellii pulchella]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FB2 OCA].
+FB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_pulchella Daboia russellii pulchella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB2 OCA].
 ==Reference==
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 [[Category: Chandra, V.]]
 [[Category: Kaur, P]]
-[[Category: Singh, T.P.]]
+[[Category: Singh, T P.]]
 [[Category: daboia russelli pulchella]]
 [[Category: neurotoxic]]
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 [[Category: structure]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:46:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:52 2008''