1x8d: Difference between revisions

Line 1:

[[Image:1x8d.gif|left|200px]]<br /><applet load="1x8d" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1x8d.gif|left|200px]]<br /><applet load="1x8d" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1x8d, resolution 1.8Å" />

'''Crystal structure of E. coli YiiL protein containing L-rhamnose'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1X8D OCA].

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==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Cho, S.J.]]

[[Category: Cho, S J.]]

[[Category: Choi, B.S.]]

[[Category: Choi, B S.]]

[[Category: Kim, J.I.]]

[[Category: Kim, J I.]]

[[Category: Lee, J.O.]]

[[Category: Lee, J O.]]

[[Category: Park, C.]]

[[Category: Park, D.]]

[[Category: Ryu, K.S.]]

[[Category: Ryu, K S.]]

[[Category: RNS]]

[[Category: l-rhamnose]]

[[Category: mutarotase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 05:53:~~30 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:02 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1x8d.gif|left|200px]]<br /><applet load="1x8d" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1x8d.gif|left|200px]]<br /><applet load="1x8d" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1x8d, resolution 1.8&Aring;" />
 '''Crystal structure of E. coli YiiL protein containing L-rhamnose'''<br />
 ==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.
+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==
-X8D 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X8D OCA].
+X8D 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==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Cho, S.J.]]
+[[Category: Cho, S J.]]
-[[Category: Choi, B.S.]]
+[[Category: Choi, B S.]]
-[[Category: Kim, J.I.]]
+[[Category: Kim, J I.]]
-[[Category: Lee, J.O.]]
+[[Category: Lee, J O.]]
 [[Category: Park, C.]]
 [[Category: Park, D.]]
-[[Category: Ryu, K.S.]]
+[[Category: Ryu, K S.]]
 [[Category: RNS]]
 [[Category: l-rhamnose]]
 [[Category: mutarotase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:53:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:02 2008''