1yxc
From Proteopedia
(New page: 200px<br /><applet load="1yxc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yxc, resolution 1.90Å" /> '''Structure of E. coli...) |
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| - | [[Image:1yxc.gif|left|200px]]<br /><applet load="1yxc" size=" | + | [[Image:1yxc.gif|left|200px]]<br /><applet load="1yxc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yxc, resolution 1.90Å" /> | caption="1yxc, resolution 1.90Å" /> | ||
'''Structure of E. coli dihydrodipicolinate synthase to 1.9 A'''<br /> | '''Structure of E. coli dihydrodipicolinate synthase to 1.9 A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction | + | Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)-lysine and meso-diaminopimelate. The activity of DHDPS is allosterically regulated by the feedback inhibitor (S)-lysine. The crystal structure of DHDPS from Escherichia coli has previously been published, but to only a resolution of 2.5 A, and the structure of the lysine-bound adduct was known to only 2.94 A resolution. Here, the crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from E. coli are presented to 1.9 and 2.0 A, respectively, resolutions that allow, in particular, more accurate definition of the protein structure. The general architecture of the active site is found to be consistent with previously determined structures, but with some important differences. Arg138, which is situated at the entrance of the active site and is thought to be involved in substrate binding, has an altered conformation and is connected via a water molecule to Tyr133 of the active-site catalytic triad. This suggests a hitherto unknown function for Arg138 in the DHDPS mechanism. Additionally, a re-evaluation of the dimer-dimer interface reveals a more extensive network of interactions than first thought. Of particular interest is the higher resolution structure of DHDPS with (S)-lysine bound at the allosteric site, which is remote to the active site, although connected to it by a chain of conserved water molecules. (S)-Lysine has a slightly altered conformation from that originally determined and does not appear to alter the DHDPS structure as others have reported. |
==About this Structure== | ==About this Structure== | ||
| - | 1YXC 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 K and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] Full crystallographic information is available from [http:// | + | 1YXC 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=K:'>K</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dobson, R | + | [[Category: Dobson, R C.J.]] |
| - | [[Category: Gerrard, J | + | [[Category: Gerrard, J A.]] |
| - | [[Category: Griffin, M | + | [[Category: Griffin, M D.W.]] |
| - | [[Category: Jameson, G | + | [[Category: Jameson, G B.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: K]] | [[Category: K]] | ||
[[Category: dihydrodipicolinate synthase]] | [[Category: dihydrodipicolinate synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:11 2008'' |
Revision as of 14:10, 21 February 2008
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Structure of E. coli dihydrodipicolinate synthase to 1.9 A
Overview
Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)-lysine and meso-diaminopimelate. The activity of DHDPS is allosterically regulated by the feedback inhibitor (S)-lysine. The crystal structure of DHDPS from Escherichia coli has previously been published, but to only a resolution of 2.5 A, and the structure of the lysine-bound adduct was known to only 2.94 A resolution. Here, the crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from E. coli are presented to 1.9 and 2.0 A, respectively, resolutions that allow, in particular, more accurate definition of the protein structure. The general architecture of the active site is found to be consistent with previously determined structures, but with some important differences. Arg138, which is situated at the entrance of the active site and is thought to be involved in substrate binding, has an altered conformation and is connected via a water molecule to Tyr133 of the active-site catalytic triad. This suggests a hitherto unknown function for Arg138 in the DHDPS mechanism. Additionally, a re-evaluation of the dimer-dimer interface reveals a more extensive network of interactions than first thought. Of particular interest is the higher resolution structure of DHDPS with (S)-lysine bound at the allosteric site, which is remote to the active site, although connected to it by a chain of conserved water molecules. (S)-Lysine has a slightly altered conformation from that originally determined and does not appear to alter the DHDPS structure as others have reported.
About this Structure
1YXC is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Dihydrodipicolinate synthase, with EC number 4.2.1.52 Full crystallographic information is available from OCA.
Reference
The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance., Dobson RC, Griffin MD, Jameson GB, Gerrard JA, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1116-24. Epub 2005, Jul 20. PMID:16041077
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