1urp: Difference between revisions

Revision as of 16:27, 21 February 2008

D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI

OverviewOverview

Conformational changes are necessary for the function of bacterial periplasmic receptors in chemotaxis and transport. Such changes allow entry and exit of ligand, and enable the correct interaction of the ligand-bound proteins with the membrane components of each system. Three open, ligand-free forms of the Escherichia coli ribose-binding protein were observed here by X-ray crystallographic studies. They are opened by 43 degrees, 50 degrees and 64 degrees with respect to the ligand-bound protein reported previously. The three open forms are not distinct, but show a clear relationship to each other. All are the product of a similar opening motion, and are stabilized by a new, almost identical packing interface between the domains. The changes are generated by similar bond rotations, although some differences in the three hinge segments are needed to accommodate the various structural scenarios. Some local repacking also occurs as interdomain contacts are lost. The least open (43 degrees) form is probably the dominant one in solution under normal conditions, although a mixture of species seems likely. The open and closed forms have distinct surfaces in the regions known to be important in chemotaxis and transport, which will differentiate their interactions with the membrane components. It seems certain that the conformational path that links the forms described here is that followed during ligand retrieval, and in ligand release into the membrane-bound permease system.

About this StructureAbout this Structure

1URP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Multiple open forms of ribose-binding protein trace the path of its conformational change., Bjorkman AJ, Mowbray SL, J Mol Biol. 1998 Jun 12;279(3):651-64. PMID:9641984

Page seeded by OCA on Thu Feb 21 15:27:36 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1urp.gif|left|200px]]<br /><applet load="1urp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1urp.gif|left|200px]]<br /><applet load="1urp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1urp, resolution 2.3&Aring;" />
 '''D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI'''<br />
 ==Overview==
-Conformational changes are necessary for the function of bacterial, periplasmic receptors in chemotaxis and transport. Such changes allow, entry and exit of ligand, and enable the correct interaction of the, ligand-bound proteins with the membrane components of each system. Three, open, ligand-free forms of the Escherichia coli ribose-binding protein, were observed here by X-ray crystallographic studies. They are opened by, 43 degrees, 50 degrees and 64 degrees with respect to the ligand-bound, protein reported previously. The three open forms are not distinct, but, show a clear relationship to each other. All are the product of a similar, opening motion, and are stabilized by a new, almost identical packing, interface between the domains. The changes are generated by similar bond, rotations, although some differences in the three hinge segments are, needed to accommodate the various structural scenarios. Some local, repacking also occurs as interdomain contacts are lost. The least open (43, degrees) form is probably the dominant one in solution under normal, conditions, although a mixture of species seems likely. The open and, closed forms have distinct surfaces in the regions known to be important, in chemotaxis and transport, which will differentiate their interactions, with the membrane components. It seems certain that the conformational, path that links the forms described here is that followed during ligand, retrieval, and in ligand release into the membrane-bound permease system.
+Conformational changes are necessary for the function of bacterial periplasmic receptors in chemotaxis and transport. Such changes allow entry and exit of ligand, and enable the correct interaction of the ligand-bound proteins with the membrane components of each system. Three open, ligand-free forms of the Escherichia coli ribose-binding protein were observed here by X-ray crystallographic studies. They are opened by 43 degrees, 50 degrees and 64 degrees with respect to the ligand-bound protein reported previously. The three open forms are not distinct, but show a clear relationship to each other. All are the product of a similar opening motion, and are stabilized by a new, almost identical packing interface between the domains. The changes are generated by similar bond rotations, although some differences in the three hinge segments are needed to accommodate the various structural scenarios. Some local repacking also occurs as interdomain contacts are lost. The least open (43 degrees) form is probably the dominant one in solution under normal conditions, although a mixture of species seems likely. The open and closed forms have distinct surfaces in the regions known to be important in chemotaxis and transport, which will differentiate their interactions with the membrane components. It seems certain that the conformational path that links the forms described here is that followed during ligand retrieval, and in ligand release into the membrane-bound permease system.
 ==About this Structure==
-URP 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=1URP OCA].
+URP 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=1URP OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Bjorkman, A.J.]]
+[[Category: Bjorkman, A J.]]
-[[Category: Mowbray, S.L.]]
+[[Category: Mowbray, S L.]]
 [[Category: chemotaxis]]
 [[Category: periplasm]]
 [[Category: transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:17:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:36 2008''