1gcg: Difference between revisions

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

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

caption="1gcg, resolution 1.9Å" />

'''THE 1.9 ANGSTROMS X-RAY STRUCTURE OF A CLOSED UNLIGANDED FORM OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUM'''<br />

==Overview==

The three-dimensional structure of a ligand-free closed form of the, glucose/galactose binding protein from Salmonella typhimurium has been, determined at a resolution of 1.9 A. The crystallographic R-factor for the, refined structure is 17.9%. The model contains all the atoms of the 309, residues of the protein sequence, a calcium ion, and 174 water molecules., The root mean square (r.m.s.) deviations for the whole molecule are: 0.010, A for bond lengths and 2.44 degrees for bond angles, indicating a good, stereochemistry for the model. This structure shows that the protein is, able to close in the absence of ligand, adopting a conformation similar to, the liganded form but slightly more open. Water molecules satisfy the, hydrogen bonding ability of the hydrophilic side chains of the binding, site in a manner which is reminiscent of the sugars' hydrogen-bonding, patterns. Since packing forces are weak, the crystallization event is, unlikely to trigger a change from an open to a closed conformation., Instead, the latter must be one of the species in equilibrium in solution, which is selected by packing in the crystal lattice.

The three-dimensional structure of a ligand-free closed form of the glucose/galactose binding protein from Salmonella typhimurium has been determined at a resolution of 1.9 A. The crystallographic R-factor for the refined structure is 17.9%. The model contains all the atoms of the 309 residues of the protein sequence, a calcium ion, and 174 water molecules. The root mean square (r.m.s.) deviations for the whole molecule are: 0.010 A for bond lengths and 2.44 degrees for bond angles, indicating a good stereochemistry for the model. This structure shows that the protein is able to close in the absence of ligand, adopting a conformation similar to the liganded form but slightly more open. Water molecules satisfy the hydrogen bonding ability of the hydrophilic side chains of the binding site in a manner which is reminiscent of the sugars' hydrogen-bonding patterns. Since packing forces are weak, the crystallization event is unlikely to trigger a change from an open to a closed conformation. Instead, the latter must be one of the species in equilibrium in solution which is selected by packing in the crystal lattice.

==About this Structure==

1GCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1GCG OCA].

1GCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCG OCA].

==Reference==

Line 13:

[[Category: Salmonella typhimurium]]

[[Category: Single protein]]

[[Category: Flocco, M.M.]]

[[Category: Flocco, M M.]]

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

[[Category: Mowbray, S L.]]

[[Category: CA]]

[[Category: galactose-binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:56:~~21 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1gcg.jpg|left|200px]]<br /><applet load="1gcg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gcg.jpg|left|200px]]<br /><applet load="1gcg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gcg, resolution 1.9&Aring;" />
 '''THE 1.9 ANGSTROMS X-RAY STRUCTURE OF A CLOSED UNLIGANDED FORM OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUM'''<br />
 ==Overview==
-The three-dimensional structure of a ligand-free closed form of the, glucose/galactose binding protein from Salmonella typhimurium has been, determined at a resolution of 1.9 A. The crystallographic R-factor for the, refined structure is 17.9%. The model contains all the atoms of the 309, residues of the protein sequence, a calcium ion, and 174 water molecules., The root mean square (r.m.s.) deviations for the whole molecule are: 0.010, A for bond lengths and 2.44 degrees for bond angles, indicating a good, stereochemistry for the model. This structure shows that the protein is, able to close in the absence of ligand, adopting a conformation similar to, the liganded form but slightly more open. Water molecules satisfy the, hydrogen bonding ability of the hydrophilic side chains of the binding, site in a manner which is reminiscent of the sugars' hydrogen-bonding, patterns. Since packing forces are weak, the crystallization event is, unlikely to trigger a change from an open to a closed conformation., Instead, the latter must be one of the species in equilibrium in solution, which is selected by packing in the crystal lattice.
+The three-dimensional structure of a ligand-free closed form of the glucose/galactose binding protein from Salmonella typhimurium has been determined at a resolution of 1.9 A. The crystallographic R-factor for the refined structure is 17.9%. The model contains all the atoms of the 309 residues of the protein sequence, a calcium ion, and 174 water molecules. The root mean square (r.m.s.) deviations for the whole molecule are: 0.010 A for bond lengths and 2.44 degrees for bond angles, indicating a good stereochemistry for the model. This structure shows that the protein is able to close in the absence of ligand, adopting a conformation similar to the liganded form but slightly more open. Water molecules satisfy the hydrogen bonding ability of the hydrophilic side chains of the binding site in a manner which is reminiscent of the sugars' hydrogen-bonding patterns. Since packing forces are weak, the crystallization event is unlikely to trigger a change from an open to a closed conformation. Instead, the latter must be one of the species in equilibrium in solution which is selected by packing in the crystal lattice.
 ==About this Structure==
-GCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GCG OCA].
+GCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCG OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Salmonella typhimurium]]
 [[Category: Single protein]]
-[[Category: Flocco, M.M.]]
+[[Category: Flocco, M M.]]
-[[Category: Mowbray, S.L.]]
+[[Category: Mowbray, S L.]]
 [[Category: CA]]
 [[Category: galactose-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:56:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:38 2008''