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| | {{STRUCTURE_1si9| PDB=1si9 | SCENE= }} | | {{STRUCTURE_1si9| PDB=1si9 | SCENE= }} |
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| - | '''Boiling stable protein isolated from Populus tremula'''
| + | ===Boiling stable protein isolated from Populus tremula=== |
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| - | ==Overview==
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| - | We previously reported on a new boiling stable protein isolated from aspen plants (Populus tremula), which we named SP1. SP1 is a stress-related protein with no significant sequence homology to other stress-related proteins. It is a 108-amino-acid hydrophilic polypeptide with a molecular mass of 12.4 kDa (Wang, W. X., Pelah, D., Alergand, T., Shoseyov, O., and Altman, A. (2002) Plant Physiol. 130, 865-875) and is found in an oligomeric form. Preliminary electron microscopy studies and matrix-assisted laser desorption ionization time-of-flight mass spectrometry experiments showed that SP1 is a dodecamer composed of two stacking hexamers. We performed a SDS-PAGE analysis, a differential scanning calorimetric study, and crystal structure determination to further characterize SP1. SDS-PAGE indicated a spontaneous assembly of SP1 to one stable oligomeric form, a dodecamer. Differential scanning calorimetric showed that SP1 has high thermostability i.e. Tm of 107 degrees C (at pH 7.8). The crystal structure of SP1 was initially determined to 2.4 A resolution by multi-wavelength anomalous dispersion method from a crystal belonging to the space group I422. The phases were extended to 1.8 A resolution using data from a different crystal form (P21). The final refined molecule includes 106 of the 108 residues and 132 water molecules (on average for each chain). The R-free is 20.1%. The crystal structure indicated that the SP1 molecule has a ferredoxin-like fold. Strong interactions between each two molecules create a stable dimer. Six dimers associate to form a ring-like-shaped dodecamer strongly resembling the particle visualized in the electron microscopy studies. No structural similarity was found between the crystal structure of SP1 and the crystal structure of other stress-related proteins such as small heat shock proteins, whose structure has been already determined. This structural study further supports our previous report that SP1 may represent a new family of stress-related proteins with high thermostability and oligomerization.
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| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15371455 is the PubMed ID number. |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Heat shock responsive]] | | [[Category: Heat shock responsive]] |
| | [[Category: Stress]] | | [[Category: Stress]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:44:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:45:44 2008'' |
Revision as of 12:45, 27 July 2008
Template:STRUCTURE 1si9
Boiling stable protein isolated from Populus tremula
Template:ABSTRACT PUBMED 15371455
About this Structure
1SI9 is a Single protein structure of sequence from Populus tremula. Full crystallographic information is available from OCA.
Reference
The structural basis of the thermostability of SP1, a novel plant (Populus tremula) boiling stable protein., Dgany O, Gonzalez A, Sofer O, Wang W, Zolotnitsky G, Wolf A, Shoham Y, Altman A, Wolf SG, Shoseyov O, Almog O, J Biol Chem. 2004 Dec 3;279(49):51516-23. Epub 2004 Sep 14. PMID:15371455
Page seeded by OCA on Sun Jul 27 15:45:44 2008
