1iho
From Proteopedia
(New page: 200px<br /><applet load="1iho" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iho, resolution 1.70Å" /> '''CRYSTAL APO-STRUCTUR...) |
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| - | [[Image:1iho.gif|left|200px]]<br /><applet load="1iho" size=" | + | [[Image:1iho.gif|left|200px]]<br /><applet load="1iho" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iho, resolution 1.70Å" /> | caption="1iho, resolution 1.70Å" /> | ||
'''CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI'''<br /> | '''CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the | + | BACKGROUND: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the pathway of pantothenate (vitamin B(5)) synthesis. It catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction. RESULTS: We describe the overexpression, purification, and crystal structure of recombinant pantothenate synthetase from E. coli. The structure was solved by a selenomethionine multiwavelength anomalous dispersion experiment and refined against native data to a final R(cryst) of 22.6% (R(free) = 24.9%) at 1.7 A resolution. The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a Rossmann fold, contains the active site cavity, with the C-terminal domain forming a hinged lid. CONCLUSIONS: The N-terminal domain is structurally very similar to class I aminoacyl-tRNA synthetases and is thus a member of the cytidylyltransferase superfamily. This relationship has been used to suggest the location of the ATP and pantoate binding sites and the nature of hinge bending that leads to the ternary enzyme-pantoate-ATP complex. |
==About this Structure== | ==About this Structure== | ||
| - | 1IHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TRS and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pantoate--beta-alanine_ligase Pantoate--beta-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.1 6.3.2.1] Full crystallographic information is available from [http:// | + | 1IHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pantoate--beta-alanine_ligase Pantoate--beta-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.1 6.3.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Abell, C.]] | [[Category: Abell, C.]] | ||
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L.]] |
| - | [[Category: Delft, F | + | [[Category: Delft, F von.]] |
[[Category: Dhanaraj, V.]] | [[Category: Dhanaraj, V.]] | ||
[[Category: Lewendon, A.]] | [[Category: Lewendon, A.]] | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:56 2008'' |
Revision as of 11:11, 21 February 2008
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CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI
Overview
BACKGROUND: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the pathway of pantothenate (vitamin B(5)) synthesis. It catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction. RESULTS: We describe the overexpression, purification, and crystal structure of recombinant pantothenate synthetase from E. coli. The structure was solved by a selenomethionine multiwavelength anomalous dispersion experiment and refined against native data to a final R(cryst) of 22.6% (R(free) = 24.9%) at 1.7 A resolution. The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a Rossmann fold, contains the active site cavity, with the C-terminal domain forming a hinged lid. CONCLUSIONS: The N-terminal domain is structurally very similar to class I aminoacyl-tRNA synthetases and is thus a member of the cytidylyltransferase superfamily. This relationship has been used to suggest the location of the ATP and pantoate binding sites and the nature of hinge bending that leads to the ternary enzyme-pantoate-ATP complex.
About this Structure
1IHO is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Pantoate--beta-alanine ligase, with EC number 6.3.2.1 Full crystallographic information is available from OCA.
Reference
The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily., von Delft F, Lewendon A, Dhanaraj V, Blundell TL, Abell C, Smith AG, Structure. 2001 May 9;9(5):439-50. PMID:11377204
Page seeded by OCA on Thu Feb 21 13:11:56 2008
Categories: Escherichia coli | Pantoate--beta-alanine ligase | Single protein | Abell, C. | Blundell, T L. | Delft, F von. | Dhanaraj, V. | Lewendon, A. | Smith, A. | EDO | TRS | Apo | Dimer | Flexible domains | High | Ksmks | Multidomain | Rossman fold
