1x9i
From Proteopedia
(New page: 200px<br /><applet load="1x9i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x9i, resolution 1.16Å" /> '''Crystal structure of...) |
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| - | [[Image:1x9i.jpg|left|200px]]<br /><applet load="1x9i" size=" | + | [[Image:1x9i.jpg|left|200px]]<br /><applet load="1x9i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1x9i, resolution 1.16Å" /> | caption="1x9i, resolution 1.16Å" /> | ||
'''Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate'''<br /> | '''Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a dual-specificity phosphoglucose/phosphomannose | + | The crystal structure of a dual-specificity phosphoglucose/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has been determined in complex with glucose 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of mannose 6-phosphate (M6P) into the active site of the enzyme shows that the PMI activity of this enzyme may be due to the additional space imparted by a threonine. In PGIs from bacterial and eukaryotic sources, which cannot use M6P as a substrate, the equivalent residue is a glutamine. The increased space may permit rotation of the C2-C3 bond in M6P to facilitate abstraction of a proton from C2 by Glu203 and, after a further C2-C3 rotation of the resulting cis-enediolate, re-donation of a proton to C1 by the same residue. A proline residue (in place of a glycine in PGI) may also promote PMI activity by positioning the C1-O1 region of M6P. Thus, the PMI reaction in PaPGI/PMI probably uses a cis-enediol mechanism of catalysis, and this activity appears to arise from a subtle difference in the architecture of the enzyme, compared to bacterial and eukaryotic PGIs. |
==About this Structure== | ==About this Structure== | ||
| - | 1X9I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with G6Q and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1X9I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=G6Q:'>G6Q</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hansen, T]] | [[Category: Hansen, T]] | ||
[[Category: Schoenheit, P.]] | [[Category: Schoenheit, P.]] | ||
| - | [[Category: Swan, M | + | [[Category: Swan, M K.]] |
[[Category: G6Q]] | [[Category: G6Q]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: pgi superfamily]] | [[Category: pgi superfamily]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:30 2008'' |
Revision as of 13:52, 21 February 2008
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Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate
Overview
The crystal structure of a dual-specificity phosphoglucose/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has been determined in complex with glucose 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of mannose 6-phosphate (M6P) into the active site of the enzyme shows that the PMI activity of this enzyme may be due to the additional space imparted by a threonine. In PGIs from bacterial and eukaryotic sources, which cannot use M6P as a substrate, the equivalent residue is a glutamine. The increased space may permit rotation of the C2-C3 bond in M6P to facilitate abstraction of a proton from C2 by Glu203 and, after a further C2-C3 rotation of the resulting cis-enediolate, re-donation of a proton to C1 by the same residue. A proline residue (in place of a glycine in PGI) may also promote PMI activity by positioning the C1-O1 region of M6P. Thus, the PMI reaction in PaPGI/PMI probably uses a cis-enediol mechanism of catalysis, and this activity appears to arise from a subtle difference in the architecture of the enzyme, compared to bacterial and eukaryotic PGIs.
About this Structure
1X9I is a Single protein structure of sequence from Pyrobaculum aerophilum with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes., Swan MK, Hansen T, Schonheit P, Davies C, Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:15518558
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