From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1tr0.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1tr0.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1tr0| PDB=1tr0 | SCENE= }} | | {{STRUCTURE_1tr0| PDB=1tr0 | SCENE= }} |
| | | | |
| - | '''Crystal Structure of a boiling stable protein SP1'''
| + | ===Crystal Structure of a boiling stable protein SP1=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15371455}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15371455 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15371455}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Sofer, O.]] | | [[Category: Sofer, O.]] |
| | [[Category: Plant protein]] | | [[Category: Plant protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:16:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:43:24 2008'' |
Revision as of 04:43, 28 July 2008
Template:STRUCTURE 1tr0
Crystal Structure of a boiling stable protein SP1
Template:ABSTRACT PUBMED 15371455
About this Structure
1TR0 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 Mon Jul 28 07:43:24 2008
