1n2a: Difference between revisions

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[[Image:1n2a.jpg|left|200px]]<br /><applet load="1n2a" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1n2a.jpg|left|200px]]<br /><applet load="1n2a" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1n2a, resolution 1.90Å" />

'''Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site'''<br />

==Overview==

Multiple sequence alignments of the eight glutathione (GSH) transferase, homologues encoded in the genome of Escherichia coli were used to define a, consensus sequence for the proteins. The consensus sequence was analyzed, in the context of the three-dimensional structure of the gst gene product, (EGST) obtained from two different crystal forms of the enzyme. The enzyme, consists of two domains. The N-terminal region (domain I) has a, thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II), is all alpha-helical. The majority of the consensus residues (12/17), reside in the N-terminal domain. Fifteen of the 17 residues are involved, in hydrophobic core interactions, turns, or electrostatic interactions, between the two domains. The results suggest that all of the homologues, retain a well-defined group of structural elements both in and between the, N-terminal alpha/beta domain and the C-terminal domain. The conservation, of two key residues for the recognition motif for the, gamma-glutamyl-portion of GSH indicates that the homologues may interact, with GSH or GSH analogues such as glutathionylspermidine or alpha-amino, acids. The genome context of two of the homologues forms the basis for a, hypothesis that the b2989 and yibF gene products are involved in, glutathionylspermidine and selenium biochemistry, respectively.

Multiple sequence alignments of the eight glutathione (GSH) transferase homologues encoded in the genome of Escherichia coli were used to define a consensus sequence for the proteins. The consensus sequence was analyzed in the context of the three-dimensional structure of the gst gene product (EGST) obtained from two different crystal forms of the enzyme. The enzyme consists of two domains. The N-terminal region (domain I) has a thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II) is all alpha-helical. The majority of the consensus residues (12/17) reside in the N-terminal domain. Fifteen of the 17 residues are involved in hydrophobic core interactions, turns, or electrostatic interactions between the two domains. The results suggest that all of the homologues retain a well-defined group of structural elements both in and between the N-terminal alpha/beta domain and the C-terminal domain. The conservation of two key residues for the recognition motif for the gamma-glutamyl-portion of GSH indicates that the homologues may interact with GSH or GSH analogues such as glutathionylspermidine or alpha-amino acids. The genome context of two of the homologues forms the basis for a hypothesis that the b2989 and yibF gene products are involved in glutathionylspermidine and selenium biochemistry, respectively.

==About this Structure==

1N2A 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 GTS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1N2A OCA].

1N2A 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=GTS:'>GTS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N2A OCA].

==Reference==

Line 14:

[[Category: Glutathione transferase]]

[[Category: Single protein]]

[[Category: Armstrong, R.N.]]

[[Category: Armstrong, R N.]]

[[Category: Gilliland, G.L.]]

[[Category: Gilliland, G L.]]

[[Category: Parsons, J.F.]]

[[Category: Parsons, J F.]]

[[Category: Rife, C.L.]]

[[Category: Rife, C L.]]

[[Category: Xiao, G.]]

[[Category: GTS]]

[[Category: transferase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 21:53:~~16 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:30 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1n2a.jpg|left|200px]]<br /><applet load="1n2a" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1n2a.jpg|left|200px]]<br /><applet load="1n2a" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1n2a, resolution 1.90&Aring;" />
 '''Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site'''<br />
 ==Overview==
-Multiple sequence alignments of the eight glutathione (GSH) transferase, homologues encoded in the genome of Escherichia coli were used to define a, consensus sequence for the proteins. The consensus sequence was analyzed, in the context of the three-dimensional structure of the gst gene product, (EGST) obtained from two different crystal forms of the enzyme. The enzyme, consists of two domains. The N-terminal region (domain I) has a, thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II), is all alpha-helical. The majority of the consensus residues (12/17), reside in the N-terminal domain. Fifteen of the 17 residues are involved, in hydrophobic core interactions, turns, or electrostatic interactions, between the two domains. The results suggest that all of the homologues, retain a well-defined group of structural elements both in and between the, N-terminal alpha/beta domain and the C-terminal domain. The conservation, of two key residues for the recognition motif for the, gamma-glutamyl-portion of GSH indicates that the homologues may interact, with GSH or GSH analogues such as glutathionylspermidine or alpha-amino, acids. The genome context of two of the homologues forms the basis for a, hypothesis that the b2989 and yibF gene products are involved in, glutathionylspermidine and selenium biochemistry, respectively.
+Multiple sequence alignments of the eight glutathione (GSH) transferase homologues encoded in the genome of Escherichia coli were used to define a consensus sequence for the proteins. The consensus sequence was analyzed in the context of the three-dimensional structure of the gst gene product (EGST) obtained from two different crystal forms of the enzyme. The enzyme consists of two domains. The N-terminal region (domain I) has a thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II) is all alpha-helical. The majority of the consensus residues (12/17) reside in the N-terminal domain. Fifteen of the 17 residues are involved in hydrophobic core interactions, turns, or electrostatic interactions between the two domains. The results suggest that all of the homologues retain a well-defined group of structural elements both in and between the N-terminal alpha/beta domain and the C-terminal domain. The conservation of two key residues for the recognition motif for the gamma-glutamyl-portion of GSH indicates that the homologues may interact with GSH or GSH analogues such as glutathionylspermidine or alpha-amino acids. The genome context of two of the homologues forms the basis for a hypothesis that the b2989 and yibF gene products are involved in glutathionylspermidine and selenium biochemistry, respectively.
 ==About this Structure==
-N2A 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 GTS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N2A OCA].
+N2A 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=GTS:'>GTS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N2A OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Glutathione transferase]]
 [[Category: Single protein]]
-[[Category: Armstrong, R.N.]]
+[[Category: Armstrong, R N.]]
-[[Category: Gilliland, G.L.]]
+[[Category: Gilliland, G L.]]
-[[Category: Parsons, J.F.]]
+[[Category: Parsons, J F.]]
-[[Category: Rife, C.L.]]
+[[Category: Rife, C L.]]
 [[Category: Xiao, G.]]
 [[Category: GTS]]
 [[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:53:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:30 2008''