1eg7
From Proteopedia
(New page: 200px<br /><applet load="1eg7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eg7, resolution 2.50Å" /> '''THE CRYSTAL STRUCTUR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1eg7.jpg|left|200px]]<br /><applet load="1eg7" size=" | + | [[Image:1eg7.jpg|left|200px]]<br /><applet load="1eg7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eg7, resolution 2.50Å" /> | caption="1eg7, resolution 2.50Å" /> | ||
'''THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA'''<br /> | '''THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure was solved at 2.5 A resolution using multiwavelength | + | The structure was solved at 2.5 A resolution using multiwavelength anomalous dispersion (MAD) scattering by Se-Met residues. The subunit of N(10)-formyltetrahydrofolate synthetase is composed of three domains organized around three mixed beta-sheets. There are two cavities between adjacent domains. One of them was identified as the nucleotide binding site by homology modeling. The large domain contains a seven-stranded beta-sheet surrounded by helices on both sides. The second domain contains a five-stranded beta-sheet with two alpha-helices packed on one side while the other two are a wall of the active site cavity. The third domain contains a four-stranded beta-sheet forming a half-barrel. The concave side is covered by two helices while the convex side is another wall of the large cavity. Arg 97 is likely involved in formyl phosphate binding. The tetrameric molecule is relatively flat with the shape of the letter X, and the active sites are located at the end of the subunits far from the subunit interface. |
==About this Structure== | ==About this Structure== | ||
| - | 1EG7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Formate--tetrahydrofolate_ligase Formate--tetrahydrofolate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.3 6.3.4.3] Full crystallographic information is available from [http:// | + | 1EG7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Formate--tetrahydrofolate_ligase Formate--tetrahydrofolate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.3 6.3.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG7 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Moorella thermoacetica]] | [[Category: Moorella thermoacetica]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dunlap, R | + | [[Category: Dunlap, R B.]] |
[[Category: Lebioda, L.]] | [[Category: Lebioda, L.]] | ||
| - | [[Category: Lovell, C | + | [[Category: Lovell, C R.]] |
[[Category: Minor, W.]] | [[Category: Minor, W.]] | ||
| - | [[Category: Odom, J | + | [[Category: Odom, J D.]] |
[[Category: Radfar, R.]] | [[Category: Radfar, R.]] | ||
| - | [[Category: Sheldrick, G | + | [[Category: Sheldrick, G M.]] |
[[Category: Shin, R.]] | [[Category: Shin, R.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 29: | Line 29: | ||
[[Category: synthetase]] | [[Category: synthetase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:27 2008'' |
Revision as of 10:27, 21 February 2008
|
THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA
Overview
The structure was solved at 2.5 A resolution using multiwavelength anomalous dispersion (MAD) scattering by Se-Met residues. The subunit of N(10)-formyltetrahydrofolate synthetase is composed of three domains organized around three mixed beta-sheets. There are two cavities between adjacent domains. One of them was identified as the nucleotide binding site by homology modeling. The large domain contains a seven-stranded beta-sheet surrounded by helices on both sides. The second domain contains a five-stranded beta-sheet with two alpha-helices packed on one side while the other two are a wall of the active site cavity. The third domain contains a four-stranded beta-sheet forming a half-barrel. The concave side is covered by two helices while the convex side is another wall of the large cavity. Arg 97 is likely involved in formyl phosphate binding. The tetrameric molecule is relatively flat with the shape of the letter X, and the active sites are located at the end of the subunits far from the subunit interface.
About this Structure
1EG7 is a Single protein structure of sequence from Moorella thermoacetica with as ligand. Active as Formate--tetrahydrofolate ligase, with EC number 6.3.4.3 Full crystallographic information is available from OCA.
Reference
The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica., Radfar R, Shin R, Sheldrick GM, Minor W, Lovell CR, Odom JD, Dunlap RB, Lebioda L, Biochemistry. 2000 Apr 11;39(14):3920-6. PMID:10747779
Page seeded by OCA on Thu Feb 21 12:27:27 2008
