1xbv
From Proteopedia
(New page: 200px<br /><applet load="1xbv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xbv, resolution 1.66Å" /> '''Crystal structure of...) |
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| - | [[Image:1xbv.gif|left|200px]]<br /><applet load="1xbv" size=" | + | [[Image:1xbv.gif|left|200px]]<br /><applet load="1xbv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xbv, resolution 1.66Å" /> | caption="1xbv, resolution 1.66Å" /> | ||
'''Crystal structure of 3-keto-L-gulonate 6-phosphate decarboxylase with bound D-ribulose 5-phosphate'''<br /> | '''Crystal structure of 3-keto-L-gulonate 6-phosphate decarboxylase with bound D-ribulose 5-phosphate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and | + | 3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-hex-3-ulose 6-phosphate synthase (HPS), members of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily, catalyze reactions that involve the formation of Mg(2+)-ion stabilized 1,2-enediolate intermediates. The active sites of KGPDC and HPS share several conserved residues, including the presumed ligands for the Mg(2+) and a catalytic histidine residue that has been implicated in protonation of the intermediate in the KGPDC-catalyzed reaction. As reported in the previous manuscript, both enzymes are naturally promiscuous, with KGPDC from Escherichia coli catalyzing a low level of the HPS reaction and the HPS from Methylomonas aminofaciens catalyzing a significant level of the KGPDC reaction. Interestingly, the promiscuous HPS reaction catalyzed by KGPDC can be significantly enhanced by replacing no more than four active site residues from KGPDC reaction with residues from HPS. In this manuscript, we report structural studies of wild-type and mutant KDGPC's that provide a structural explanation for both the natural promiscuity for the HPS reaction and the enhanced HPS activity and diminished KGPDC activity catalyzed by active site mutants. |
==About this Structure== | ==About this Structure== | ||
| - | 1XBV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with 5RP and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XBV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=5RP:'>5RP</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Akana, J.]] | [[Category: Akana, J.]] | ||
| - | [[Category: Gerlt, J | + | [[Category: Gerlt, J A.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Wise, E | + | [[Category: Wise, E L.]] |
| - | [[Category: Yew, W | + | [[Category: Yew, W S.]] |
[[Category: 5RP]] | [[Category: 5RP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:14 2008'' |
Revision as of 13:53, 21 February 2008
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Crystal structure of 3-keto-L-gulonate 6-phosphate decarboxylase with bound D-ribulose 5-phosphate
Overview
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-hex-3-ulose 6-phosphate synthase (HPS), members of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily, catalyze reactions that involve the formation of Mg(2+)-ion stabilized 1,2-enediolate intermediates. The active sites of KGPDC and HPS share several conserved residues, including the presumed ligands for the Mg(2+) and a catalytic histidine residue that has been implicated in protonation of the intermediate in the KGPDC-catalyzed reaction. As reported in the previous manuscript, both enzymes are naturally promiscuous, with KGPDC from Escherichia coli catalyzing a low level of the HPS reaction and the HPS from Methylomonas aminofaciens catalyzing a significant level of the KGPDC reaction. Interestingly, the promiscuous HPS reaction catalyzed by KGPDC can be significantly enhanced by replacing no more than four active site residues from KGPDC reaction with residues from HPS. In this manuscript, we report structural studies of wild-type and mutant KDGPC's that provide a structural explanation for both the natural promiscuity for the HPS reaction and the enhanced HPS activity and diminished KGPDC activity catalyzed by active site mutants.
About this Structure
1XBV is a Protein complex structure of sequences from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase., Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I, Biochemistry. 2005 Feb 15;44(6):1816-23. PMID:15697207
Page seeded by OCA on Thu Feb 21 15:53:14 2008
Categories: Escherichia coli | Protein complex | Akana, J. | Gerlt, J A. | Rayment, I. | Wise, E L. | Yew, W S. | 5RP | MG | Beta/alpha barrel | Tim barrel
