2i5p
From Proteopedia
(New page: 200px<br /><applet load="2i5p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i5p, resolution 2.30Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2i5p.gif|left|200px]]<br /><applet load="2i5p" size=" | + | [[Image:2i5p.gif|left|200px]]<br /><applet load="2i5p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2i5p, resolution 2.30Å" /> | caption="2i5p, resolution 2.30Å" /> | ||
'''Crystal structure of glyceraldehyde-3-phosphate dehydrogenase isoform 1 from K. marxianus'''<br /> | '''Crystal structure of glyceraldehyde-3-phosphate dehydrogenase isoform 1 from K. marxianus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The presence of an isoform of glyceraldehyde-3-phosphate dehydrogenase | + | The presence of an isoform of glyceraldehyde-3-phosphate dehydrogenase (kmGAPDH1p) associated with the cell wall of a flocculent strain of Kluyveromyces marxianus was the first report of a non-cytosolic localization of a glycolytic enzyme, but the mechanism by which the protein is transported to the cell surface is not known. To identify structural features that could account for the multiple localizations of the protein, the three-dimensional structure of kmGAPDH1p was determined by x-ray crystallography and small angle x-ray scattering. The x-ray crystallographic structure of kmGAPDH1p revealed a dimer, although all GAPDH homologs studied thus far have a tetrameric structure with 222 symmetry. Interestingly, the structure of kmGAPDH1p in solution revealed a tetramer with a 70 degrees tilt angle between the dimers. Moreover, the separation between the centers of the dimers composing the kmGAPDH1p tetramer diminished from 34 to 30 A upon NAD(+) binding, this latter value being similar to the observed in the crystallographic models of GAPDH homologs. The less compact structure of apo-kmGAPDH1p could already be the first image of the transition intermediate between the tetramer observed in solution and the dimeric form found in the crystal structure, which we postulate to exist in vivo because of the protein's multiple subcellular localizations in this yeast species. |
==About this Structure== | ==About this Structure== | ||
| - | 2I5P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_marxianus Kluyveromyces marxianus] with GLC and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http:// | + | 2I5P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_marxianus Kluyveromyces marxianus] with <scene name='pdbligand=GLC:'>GLC</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I5P OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Kluyveromyces marxianus]] | [[Category: Kluyveromyces marxianus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Damas, A | + | [[Category: Damas, A M.]] |
[[Category: Ferreira-da-Silva, F.]] | [[Category: Ferreira-da-Silva, F.]] | ||
[[Category: Gales, L.]] | [[Category: Gales, L.]] | ||
[[Category: Moradas-Ferreira, P.]] | [[Category: Moradas-Ferreira, P.]] | ||
| - | [[Category: Pereira, P | + | [[Category: Pereira, P J.B.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: GLC]] | [[Category: GLC]] | ||
| Line 26: | Line 26: | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:49:19 2008'' |
Revision as of 15:49, 21 February 2008
|
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase isoform 1 from K. marxianus
Overview
The presence of an isoform of glyceraldehyde-3-phosphate dehydrogenase (kmGAPDH1p) associated with the cell wall of a flocculent strain of Kluyveromyces marxianus was the first report of a non-cytosolic localization of a glycolytic enzyme, but the mechanism by which the protein is transported to the cell surface is not known. To identify structural features that could account for the multiple localizations of the protein, the three-dimensional structure of kmGAPDH1p was determined by x-ray crystallography and small angle x-ray scattering. The x-ray crystallographic structure of kmGAPDH1p revealed a dimer, although all GAPDH homologs studied thus far have a tetrameric structure with 222 symmetry. Interestingly, the structure of kmGAPDH1p in solution revealed a tetramer with a 70 degrees tilt angle between the dimers. Moreover, the separation between the centers of the dimers composing the kmGAPDH1p tetramer diminished from 34 to 30 A upon NAD(+) binding, this latter value being similar to the observed in the crystallographic models of GAPDH homologs. The less compact structure of apo-kmGAPDH1p could already be the first image of the transition intermediate between the tetramer observed in solution and the dimeric form found in the crystal structure, which we postulate to exist in vivo because of the protein's multiple subcellular localizations in this yeast species.
About this Structure
2I5P is a Single protein structure of sequence from Kluyveromyces marxianus with and as ligands. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.
Reference
The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures., Ferreira-da-Silva F, Pereira PJ, Gales L, Roessle M, Svergun DI, Moradas-Ferreira P, Damas AM, J Biol Chem. 2006 Nov 3;281(44):33433-40. Epub 2006 Sep 7. PMID:16963457
Page seeded by OCA on Thu Feb 21 17:49:19 2008
