1txk: Difference between revisions

Line 1:

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

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

caption="1txk, resolution 2.50Å" />

'''Crystal structure of Escherichia coli OpgG'''<br />

==Overview==

Osmoregulated periplasmic glucans (OPGs) G protein (OpgG) is required for, OPGs biosynthesis. OPGs from Escherichia coli are branched glucans, with a, backbone of beta-1,2 glucose units and with branches attached by beta-1,6, linkages. In Proteobacteria, OPGs are involved in osmoprotection, biofilm, formation, virulence and resistance to antibiotics. Despite their, important biological implications, enzymes synthesizing OPGs are poorly, characterized. Here, we report the 2.5 A crystal structure of OpgG from, E.coli. The structure was solved using a selenemethionine derivative of, OpgG and the multiple anomalous diffraction method (MAD). The protein is, composed of two beta-sandwich domains connected by one turn of 3(10), helix. The N-terminal domain (residues 22-388) displays a 25-stranded, beta-sandwich fold found in several carbohydrate-related proteins. It, exhibits a large cleft comprising many aromatic and acidic residues. This, putative binding site shares some similarities with enzymes such as, galactose mutarotase and glucodextranase, suggesting a potential catalytic, role for this domain in OPG synthesis. On the other hand, the C-terminal, domain (residues 401-512) has a seven-stranded immunoglobulin-like, beta-sandwich fold, found in many proteins where it is mainly implicated, in interactions with other molecules. The structural data suggest that, OpgG is an OPG branching enzyme in which the catalytic activity is located, in the large N-terminal domain and controlled via the smaller C-terminal, domain.

Osmoregulated periplasmic glucans (OPGs) G protein (OpgG) is required for OPGs biosynthesis. OPGs from Escherichia coli are branched glucans, with a backbone of beta-1,2 glucose units and with branches attached by beta-1,6 linkages. In Proteobacteria, OPGs are involved in osmoprotection, biofilm formation, virulence and resistance to antibiotics. Despite their important biological implications, enzymes synthesizing OPGs are poorly characterized. Here, we report the 2.5 A crystal structure of OpgG from E.coli. The structure was solved using a selenemethionine derivative of OpgG and the multiple anomalous diffraction method (MAD). The protein is composed of two beta-sandwich domains connected by one turn of 3(10) helix. The N-terminal domain (residues 22-388) displays a 25-stranded beta-sandwich fold found in several carbohydrate-related proteins. It exhibits a large cleft comprising many aromatic and acidic residues. This putative binding site shares some similarities with enzymes such as galactose mutarotase and glucodextranase, suggesting a potential catalytic role for this domain in OPG synthesis. On the other hand, the C-terminal domain (residues 401-512) has a seven-stranded immunoglobulin-like beta-sandwich fold, found in many proteins where it is mainly implicated in interactions with other molecules. The structural data suggest that OpgG is an OPG branching enzyme in which the catalytic activity is located in the large N-terminal domain and controlled via the smaller C-terminal domain.

==About this Structure==

1TXK 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 NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TXK OCA].

1TXK 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=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXK OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Bohin, J.P.]]

[[Category: Bohin, J P.]]

[[Category: Clantin, B.]]

[[Category: Hanoulle, X.]]

Line 24:

[[Category: beta-sandwich]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1txk.gif|left|200px]]<br /><applet load="1txk" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1txk.gif|left|200px]]<br /><applet load="1txk" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1txk, resolution 2.50&Aring;" />
 '''Crystal structure of Escherichia coli OpgG'''<br />
 ==Overview==
-Osmoregulated periplasmic glucans (OPGs) G protein (OpgG) is required for, OPGs biosynthesis. OPGs from Escherichia coli are branched glucans, with a, backbone of beta-1,2 glucose units and with branches attached by beta-1,6, linkages. In Proteobacteria, OPGs are involved in osmoprotection, biofilm, formation, virulence and resistance to antibiotics. Despite their, important biological implications, enzymes synthesizing OPGs are poorly, characterized. Here, we report the 2.5 A crystal structure of OpgG from, E.coli. The structure was solved using a selenemethionine derivative of, OpgG and the multiple anomalous diffraction method (MAD). The protein is, composed of two beta-sandwich domains connected by one turn of 3(10), helix. The N-terminal domain (residues 22-388) displays a 25-stranded, beta-sandwich fold found in several carbohydrate-related proteins. It, exhibits a large cleft comprising many aromatic and acidic residues. This, putative binding site shares some similarities with enzymes such as, galactose mutarotase and glucodextranase, suggesting a potential catalytic, role for this domain in OPG synthesis. On the other hand, the C-terminal, domain (residues 401-512) has a seven-stranded immunoglobulin-like, beta-sandwich fold, found in many proteins where it is mainly implicated, in interactions with other molecules. The structural data suggest that, OpgG is an OPG branching enzyme in which the catalytic activity is located, in the large N-terminal domain and controlled via the smaller C-terminal, domain.
+Osmoregulated periplasmic glucans (OPGs) G protein (OpgG) is required for OPGs biosynthesis. OPGs from Escherichia coli are branched glucans, with a backbone of beta-1,2 glucose units and with branches attached by beta-1,6 linkages. In Proteobacteria, OPGs are involved in osmoprotection, biofilm formation, virulence and resistance to antibiotics. Despite their important biological implications, enzymes synthesizing OPGs are poorly characterized. Here, we report the 2.5 A crystal structure of OpgG from E.coli. The structure was solved using a selenemethionine derivative of OpgG and the multiple anomalous diffraction method (MAD). The protein is composed of two beta-sandwich domains connected by one turn of 3(10) helix. The N-terminal domain (residues 22-388) displays a 25-stranded beta-sandwich fold found in several carbohydrate-related proteins. It exhibits a large cleft comprising many aromatic and acidic residues. This putative binding site shares some similarities with enzymes such as galactose mutarotase and glucodextranase, suggesting a potential catalytic role for this domain in OPG synthesis. On the other hand, the C-terminal domain (residues 401-512) has a seven-stranded immunoglobulin-like beta-sandwich fold, found in many proteins where it is mainly implicated in interactions with other molecules. The structural data suggest that OpgG is an OPG branching enzyme in which the catalytic activity is located in the large N-terminal domain and controlled via the smaller C-terminal domain.
 ==About this Structure==
-TXK 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 NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TXK OCA].
+TXK 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=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXK OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Bohin, J.P.]]
+[[Category: Bohin, J P.]]
 [[Category: Clantin, B.]]
 [[Category: Hanoulle, X.]]
@@ Line 24: / Line 24: @@
 [[Category: beta-sandwich]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:40:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:22 2008''