1zeq: Difference between revisions

Line 1:

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

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

caption="1zeq, resolution 1.50Å" />

'''1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli'''<br />

==Overview==

We have determined the crystal structure of apo-CusF, a periplasmic, protein involved in copper and silver resistance in Escherichia coli. The, protein forms a five-stranded beta-barrel, classified as an OB-fold, which, is a unique topology for a copper-binding protein. NMR chemical shift, mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered, at one end of the beta-barrel, and their side chains are oriented toward, the interior of the barrel. Cu(I) can be modeled into the apo-CusF, structure with only minimal structural changes using H36, M47, and M49 as, ligands. The unique structure and metal binding site of CusF are distinct, from those of previously characterized copper-binding proteins.

We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded beta-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered at one end of the beta-barrel, and their side chains are oriented toward the interior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper-binding proteins.

==About this Structure==

1ZEQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ZEQ OCA].

1ZEQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZEQ OCA].

==Reference==

Line 15:

[[Category: Franke, S.]]

[[Category: Heroux, A.]]

[[Category: Loftin, I.R.]]

[[Category: Loftin, I R.]]

[[Category: McEvoy, M.M.]]

[[Category: McEvoy, M M.]]

[[Category: Montfort, W.R.]]

[[Category: Montfort, W R.]]

[[Category: Rensing, C.]]

[[Category: Roberts, S.A.]]

[[Category: Roberts, S A.]]

[[Category: Weichsel, A.]]

[[Category: beta barrel]]

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[[Category: ob-fold]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:48 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1zeq.gif|left|200px]]<br /><applet load="1zeq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zeq.gif|left|200px]]<br /><applet load="1zeq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zeq, resolution 1.50&Aring;" />
 '''1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli'''<br />
 ==Overview==
-We have determined the crystal structure of apo-CusF, a periplasmic, protein involved in copper and silver resistance in Escherichia coli. The, protein forms a five-stranded beta-barrel, classified as an OB-fold, which, is a unique topology for a copper-binding protein. NMR chemical shift, mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered, at one end of the beta-barrel, and their side chains are oriented toward, the interior of the barrel. Cu(I) can be modeled into the apo-CusF, structure with only minimal structural changes using H36, M47, and M49 as, ligands. The unique structure and metal binding site of CusF are distinct, from those of previously characterized copper-binding proteins.
+We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded beta-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered at one end of the beta-barrel, and their side chains are oriented toward the interior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper-binding proteins.
 ==About this Structure==
-ZEQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZEQ OCA].
+ZEQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZEQ OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Franke, S.]]
 [[Category: Heroux, A.]]
-[[Category: Loftin, I.R.]]
+[[Category: Loftin, I R.]]
-[[Category: McEvoy, M.M.]]
+[[Category: McEvoy, M M.]]
-[[Category: Montfort, W.R.]]
+[[Category: Montfort, W R.]]
 [[Category: Rensing, C.]]
-[[Category: Roberts, S.A.]]
+[[Category: Roberts, S A.]]
 [[Category: Weichsel, A.]]
 [[Category: beta barrel]]
@@ Line 26: / Line 26: @@
 [[Category: ob-fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:25:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:48 2008''