1m3u
From Proteopedia
(New page: 200px<br /><applet load="1m3u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3u, resolution 1.800Å" /> '''Crystal Structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1m3u.gif|left|200px]]<br /><applet load="1m3u" size=" | + | [[Image:1m3u.gif|left|200px]]<br /><applet load="1m3u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m3u, resolution 1.800Å" /> | caption="1m3u, resolution 1.800Å" /> | ||
'''Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate'''<br /> | '''Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystal structure of E. coli ketopantoate | + | We report the crystal structure of E. coli ketopantoate hydroxymethyltransferase (KPHMT) at 1.9 A resolution, in complex with its product, ketopantoate. KPHMT catalyzes the first step in the biosynthesis of pantothenate (vitamin B(5)), the precursor of coenzyme A and the acyl carrier protein cofactor. The structure of the decameric enzyme was solved by multiwavelength anomalous dispersion to locate 160 selenomethionine sites and phase 560 kDa of protein, making it the largest structure solved by this approach. KPHMT adopts the (betaalpha)(8) barrel fold and is a member of the phosphoenolpyruvate/pyruvate superfamily. The active site contains a ketopantoate bidentately coordinated to Mg(2+). Similar binding is likely for the substrate, alpha-ketoisovalerate, orienting the C3 for deprotonation. |
==About this Structure== | ==About this Structure== | ||
| - | 1M3U 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 MG and KPL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.11 2.1.2.11] Full crystallographic information is available from [http:// | + | 1M3U 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=MG:'>MG</scene> and <scene name='pdbligand=KPL:'>KPL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.11 2.1.2.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3U OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[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: Inoue, T.]] | [[Category: Inoue, T.]] | ||
| - | [[Category: Ottenhof, H | + | [[Category: Ottenhof, H H.]] |
| - | [[Category: Saldanha, S | + | [[Category: Saldanha, S A.]] |
| - | [[Category: Smith, A | + | [[Category: Smith, A G.]] |
[[Category: Witty, M.]] | [[Category: Witty, M.]] | ||
[[Category: KPL]] | [[Category: KPL]] | ||
| Line 31: | Line 31: | ||
[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:08 2008'' |
Revision as of 11:51, 21 February 2008
|
Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate
Overview
We report the crystal structure of E. coli ketopantoate hydroxymethyltransferase (KPHMT) at 1.9 A resolution, in complex with its product, ketopantoate. KPHMT catalyzes the first step in the biosynthesis of pantothenate (vitamin B(5)), the precursor of coenzyme A and the acyl carrier protein cofactor. The structure of the decameric enzyme was solved by multiwavelength anomalous dispersion to locate 160 selenomethionine sites and phase 560 kDa of protein, making it the largest structure solved by this approach. KPHMT adopts the (betaalpha)(8) barrel fold and is a member of the phosphoenolpyruvate/pyruvate superfamily. The active site contains a ketopantoate bidentately coordinated to Mg(2+). Similar binding is likely for the substrate, alpha-ketoisovalerate, orienting the C3 for deprotonation.
About this Structure
1M3U is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as 3-methyl-2-oxobutanoate hydroxymethyltransferase, with EC number 2.1.2.11 Full crystallographic information is available from OCA.
Reference
Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites., von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C, Structure. 2003 Aug;11(8):985-96. PMID:12906829
Page seeded by OCA on Thu Feb 21 13:51:08 2008
Categories: 3-methyl-2-oxobutanoate hydroxymethyltransferase | Escherichia coli | Single protein | Abell, C. | Blundell, T L. | Delft, F von. | Dhanaraj, V. | Inoue, T. | Ottenhof, H H. | Saldanha, S A. | Smith, A G. | Witty, M. | KPL | MG | Beta-alpha-barrel | Decamer | Ketopantoate | Selenomethionine mad | Tim-barrel
