2ro9: Difference between revisions

Revision as of 05:19, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ro9.png

Template:STRUCTURE 2ro9

Solution structure of calcium bound soybean calmodulin isoform 1 C-terminal domainSolution structure of calcium bound soybean calmodulin isoform 1 C-terminal domain

Template:ABSTRACT PUBMED 18347016

About this StructureAbout this Structure

2RO9 is a Single protein structure of sequence from Glycine max. Full experimental information is available from OCA.

ReferenceReference

The solution structures of two soybean calmodulin isoforms provide a structural basis for their selective target-activation properties., Ishida H, Huang H, Yamniuk AP, Takaya Y, Vogel HJ, J Biol Chem. 2008 Mar 17;. PMID:18347016

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 {{STRUCTURE_2ro9|  PDB=2ro9  |  SCENE=  }}
-'''Solution structure of calcium bound soybean calmodulin isoform 1 C-terminal domain'''
+===Solution structure of calcium bound soybean calmodulin isoform 1 C-terminal domain===
-==Overview==
+<!--
-The intracellular calcium ion is one of the most important secondary messengers in eukaryotic cells. Ca2+-signals are translated into physiological responses by EF-hand calcium binding proteins such as calmodulin (CaM). Multiple CaM isoforms occur in plant cells, while only a single CaM protein is found in animals. Soybean CaM isoform 1 (sCaM1) shares 90% amino-acid sequence identity with animal CaM (aCaM), whereas sCaM4 is only 78% identical. These two sCaM isoforms have distinct target-enzyme activation properties and physiological functions. sCaM4 is highly expressed during the plant's self-defense reaction, and activates the enzyme nitric-oxide synthase (NOS), while sCaM1 is incapable of activating NOS. The mechanism of selective target-activation by plant CaM isoforms is poorly understood. We have determined high resolution NMR solution structures of Ca2+- sCaM1 and Ca2+-sCaM4 by utilizing nuclear-Overhauser-effects and residual dipolar couplings. These were compared to previously determined Ca2+-aCaM structures. For the N-lobe of the protein, the solution structures of Ca2+-sCaM1, Ca2+-sCaM4 and Ca2+-aCaM all closely resemble each other. However, in spite of the high sequence identity with aCaM, the C-lobe of Ca2+-sCaM1 has a more open-conformation and consequently a larger hydrophobic target-protein binding pocket than Ca2+-aCaM or Ca2+-sCaM4, the presence of which was further confirmed through biophysical measurements. The single Val144 Met substitution in the C-lobe of Ca2+-sCaM1, that restores its ability to activate NOS, alters the structure of the C-lobe to a more closed-conformation resembling Ca2+-aCaM and Ca2+-sCaM4. The relationships between the structural differences in the two Ca2+-sCaM isoforms and their selective target-activation properties are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_18347016}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18347016 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18347016}}
 ==About this Structure==
-RO9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RO9 OCA].
+RO9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RO9 OCA].
 ==Reference==
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 [[Category: Target activation]]
 [[Category: Target binding]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:19:14 2008''