1dpp: Difference between revisions

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

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

caption="1dpp, resolution 3.2Å" />

'''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE'''<br />

==Overview==

The Escherichia coli periplasmic dipeptide binding protein functions in, both peptide transport and taxis toward peptides. The structure of the, dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has, been determined at 3.2 A resolution. The binding site for dipeptides is, designed to recognize the ligand's backbone while providing space to, accommodate a variety of side chains. Some repositioning of protein side, chains lining the binding site must occur when the dipeptide's second, residue is larger than leucine. The protein's fold is very similar to that, of the Salmonella typhimurium oligopeptide binding protein, and a, comparison of the structures reveals the structural basis for the, dipeptide binding protein's preference for shorter peptides.

The Escherichia coli periplasmic dipeptide binding protein functions in both peptide transport and taxis toward peptides. The structure of the dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has been determined at 3.2 A resolution. The binding site for dipeptides is designed to recognize the ligand's backbone while providing space to accommodate a variety of side chains. Some repositioning of protein side chains lining the binding site must occur when the dipeptide's second residue is larger than leucine. The protein's fold is very similar to that of the Salmonella typhimurium oligopeptide binding protein, and a comparison of the structures reveals the structural basis for the dipeptide binding protein's preference for shorter peptides.

==About this Structure==

1DPP 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=1DPP OCA].

1DPP 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=1DPP OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Dunten, P.]]

[[Category: Mowbray, S.L.]]

[[Category: Mowbray, S L.]]

[[Category: chemotaxis]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:28:~~43 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:07 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dpp.jpg|left|200px]]<br /><applet load="1dpp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dpp.jpg|left|200px]]<br /><applet load="1dpp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dpp, resolution 3.2&Aring;" />
 '''DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE'''<br />
 ==Overview==
-The Escherichia coli periplasmic dipeptide binding protein functions in, both peptide transport and taxis toward peptides. The structure of the, dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has, been determined at 3.2 A resolution. The binding site for dipeptides is, designed to recognize the ligand's backbone while providing space to, accommodate a variety of side chains. Some repositioning of protein side, chains lining the binding site must occur when the dipeptide's second, residue is larger than leucine. The protein's fold is very similar to that, of the Salmonella typhimurium oligopeptide binding protein, and a, comparison of the structures reveals the structural basis for the, dipeptide binding protein's preference for shorter peptides.
+The Escherichia coli periplasmic dipeptide binding protein functions in both peptide transport and taxis toward peptides. The structure of the dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has been determined at 3.2 A resolution. The binding site for dipeptides is designed to recognize the ligand's backbone while providing space to accommodate a variety of side chains. Some repositioning of protein side chains lining the binding site must occur when the dipeptide's second residue is larger than leucine. The protein's fold is very similar to that of the Salmonella typhimurium oligopeptide binding protein, and a comparison of the structures reveals the structural basis for the dipeptide binding protein's preference for shorter peptides.
 ==About this Structure==
-DPP 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=1DPP OCA].
+DPP 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=1DPP OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Dunten, P.]]
-[[Category: Mowbray, S.L.]]
+[[Category: Mowbray, S L.]]
 [[Category: chemotaxis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:28:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:07 2008''