1god: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1god" size="450" color="white" frame="true" align="right" spinBox="true" caption="1god, resolution 2.8Å" /> '''MONOMERIC LYS-49 PHOS...
 
No edit summary
Line 1: Line 1:
[[Image:1god.gif|left|200px]]<br /><applet load="1god" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1god.gif|left|200px]]<br /><applet load="1god" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1god, resolution 2.8&Aring;" />
caption="1god, resolution 2.8&Aring;" />
'''MONOMERIC LYS-49 PHOSPHOLIPASE A2 HOMOLOGUE ISOLATED FROM THE VENOM OF CERROPHIDION (BOTHROPS) GODMANI'''<br />
'''MONOMERIC LYS-49 PHOSPHOLIPASE A2 HOMOLOGUE ISOLATED FROM THE VENOM OF CERROPHIDION (BOTHROPS) GODMANI'''<br />


==Overview==
==Overview==
Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a, Ca2+-independent mechanism which does not involve catalytic activity. With, the aim of determining the structural basis for this novel activity, we, have solved the crystal structure of myotoxin-II, a Lys49-PLA2 isolated, from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 A, resolution by molecular replacement. The final model has been refined to a, final crystallografic residual (Rfactor) of 18.8% (Rfree = 28.2%), with, excellent stereochemistry. godMT-II is also monomeric in the crystalline, state, and small-angle X-ray scattering results demonstrate that the, protein is monomeric in solution under fisicochemical conditions similar, to those used in the crystallographic studies.
Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we have solved the crystal structure of myotoxin-II, a Lys49-PLA2 isolated from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 A resolution by molecular replacement. The final model has been refined to a final crystallografic residual (Rfactor) of 18.8% (Rfree = 28.2%), with excellent stereochemistry. godMT-II is also monomeric in the crystalline state, and small-angle X-ray scattering results demonstrate that the protein is monomeric in solution under fisicochemical conditions similar to those used in the crystallographic studies.


==About this Structure==
==About this Structure==
1GOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cerrophidion_godmani Cerrophidion godmani]. 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=1GOD OCA].  
1GOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cerrophidion_godmani Cerrophidion godmani]. 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=1GOD OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Arni, R.K.]]
[[Category: Arni, R K.]]
[[Category: Barberato, C.]]
[[Category: Barberato, C.]]
[[Category: Diaz-Oreiro, C.]]
[[Category: Diaz-Oreiro, C.]]
[[Category: Fontes, M.R.M.]]
[[Category: Fontes, M R.M.]]
[[Category: Gutierrez, J.M.]]
[[Category: Gutierrez, J M.]]
[[Category: Ward, R.J.]]
[[Category: Ward, R J.]]
[[Category: bothrops]]
[[Category: bothrops]]
[[Category: lys49-phospholipase a2]]
[[Category: lys49-phospholipase a2]]
[[Category: snake venom]]
[[Category: snake venom]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:12:07 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:14 2008''

Revision as of 13:52, 21 February 2008

File:1god.gif


1god, resolution 2.8Å

Drag the structure with the mouse to rotate

MONOMERIC LYS-49 PHOSPHOLIPASE A2 HOMOLOGUE ISOLATED FROM THE VENOM OF CERROPHIDION (BOTHROPS) GODMANI

OverviewOverview

Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we have solved the crystal structure of myotoxin-II, a Lys49-PLA2 isolated from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 A resolution by molecular replacement. The final model has been refined to a final crystallografic residual (Rfactor) of 18.8% (Rfree = 28.2%), with excellent stereochemistry. godMT-II is also monomeric in the crystalline state, and small-angle X-ray scattering results demonstrate that the protein is monomeric in solution under fisicochemical conditions similar to those used in the crystallographic studies.

About this StructureAbout this Structure

1GOD is a Single protein structure of sequence from Cerrophidion godmani. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani., Arni RK, Fontes MR, Barberato C, Gutierrez JM, Diaz C, Ward RJ, Arch Biochem Biophys. 1999 Jun 15;366(2):177-82. PMID:10356281

Page seeded by OCA on Thu Feb 21 12:52:14 2008

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

OCA