1x8d
From Proteopedia
(New page: 200px<br /><applet load="1x8d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x8d, resolution 1.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1x8d.gif|left|200px]]<br /><applet load="1x8d" size=" | + | [[Image:1x8d.gif|left|200px]]<br /><applet load="1x8d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1x8d, resolution 1.8Å" /> | caption="1x8d, resolution 1.8Å" /> | ||
'''Crystal structure of E. coli YiiL protein containing L-rhamnose'''<br /> | '''Crystal structure of E. coli YiiL protein containing L-rhamnose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Escherichia coli rhamnose mutarotase (YiiL) is | + | The crystal structure of Escherichia coli rhamnose mutarotase (YiiL) is completely different from the previously reported structures of the Lactococcus lactis galactose mutarotase and the Bacillus subtilis RbsD (pyranase). YiiL exists as a locally asymmetric dimer, which is stabilized by an intermolecular beta-sheet, various hydrophobic interactions, and a cation-pi interaction with a salt-bridge. The protein folds of YiiL are similar to those of a Streptomyces coelicolor mono-oxygenase and a hypothetical Arabidopsis thaliana protein At3g17210. By assaying the enzymatic activity of six active-site mutants and by comparing the crystal structure-derived active site conformations of YiiL, RbsD, and a galactose mutarotase, we were able to define the amino acid residues required for catalysis and suggest a possible catalytic mechanism for YiiL. Although the active-site amino acid residues of YiiL (His, Tyr, and Trp) differ greatly from those of galactose mutarotase (His, Glu, and Asp), their geometries, which determine the structures of the preferred monosaccharide substrates, are conserved. In addition, the in vivo function of YiiL was assessed by constructing a mutant E.coli strain that carries a yiiL deletion. The presence of the yiiL gene is critical for efficient cell growth only when concentrations of l-rhamnose are limited. |
==About this Structure== | ==About this Structure== | ||
| - | 1X8D 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 RNS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1X8D 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=RNS:'>RNS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X8D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cho, S | + | [[Category: Cho, S J.]] |
| - | [[Category: Choi, B | + | [[Category: Choi, B S.]] |
| - | [[Category: Kim, J | + | [[Category: Kim, J I.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J O.]] |
[[Category: Park, C.]] | [[Category: Park, C.]] | ||
[[Category: Park, D.]] | [[Category: Park, D.]] | ||
| - | [[Category: Ryu, K | + | [[Category: Ryu, K S.]] |
[[Category: RNS]] | [[Category: RNS]] | ||
[[Category: l-rhamnose]] | [[Category: l-rhamnose]] | ||
[[Category: mutarotase]] | [[Category: mutarotase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:02 2008'' |
Revision as of 13:52, 21 February 2008
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Crystal structure of E. coli YiiL protein containing L-rhamnose
Overview
The crystal structure of Escherichia coli rhamnose mutarotase (YiiL) is completely different from the previously reported structures of the Lactococcus lactis galactose mutarotase and the Bacillus subtilis RbsD (pyranase). YiiL exists as a locally asymmetric dimer, which is stabilized by an intermolecular beta-sheet, various hydrophobic interactions, and a cation-pi interaction with a salt-bridge. The protein folds of YiiL are similar to those of a Streptomyces coelicolor mono-oxygenase and a hypothetical Arabidopsis thaliana protein At3g17210. By assaying the enzymatic activity of six active-site mutants and by comparing the crystal structure-derived active site conformations of YiiL, RbsD, and a galactose mutarotase, we were able to define the amino acid residues required for catalysis and suggest a possible catalytic mechanism for YiiL. Although the active-site amino acid residues of YiiL (His, Tyr, and Trp) differ greatly from those of galactose mutarotase (His, Glu, and Asp), their geometries, which determine the structures of the preferred monosaccharide substrates, are conserved. In addition, the in vivo function of YiiL was assessed by constructing a mutant E.coli strain that carries a yiiL deletion. The presence of the yiiL gene is critical for efficient cell growth only when concentrations of l-rhamnose are limited.
About this Structure
1X8D is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase., Ryu KS, Kim JI, Cho SJ, Park D, Park C, Cheong HK, Lee JO, Choi BS, J Mol Biol. 2005 May 27;349(1):153-62. Epub 2005 Apr 7. PMID:15876375
Page seeded by OCA on Thu Feb 21 15:52:02 2008
Categories: Escherichia coli | Single protein | Cho, S J. | Choi, B S. | Kim, J I. | Lee, J O. | Park, C. | Park, D. | Ryu, K S. | RNS | L-rhamnose | Mutarotase
