1pp4: Difference between revisions

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[[Image:1pp4.gif|left|200px]]<br /><applet load="1pp4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pp4.gif|left|200px]]<br /><applet load="1pp4" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pp4, resolution 2.5Å" />

'''The crystal structure of rhamnogalacturonan acetylesterase in space group P3121'''<br />

==Overview==

The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus, aculeatus has been crystallized in two crystal forms, an orthorhombic and, a trigonal crystal form. In the orthorhombic crystal form, the covalently, bound carbohydrate at one of the two N-glycosylation sites is involved in, crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and, the trigonal crystal form at pH 4.5. In one case, the two crystal forms, were found in the same drop at pH 4.7. The differences in crystal packing, in the two crystal forms can be explained by the pH-dependent variation in, the protonation state of the glutamic acid residues on the protein, surface.

The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface.

==About this Structure==

1PP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PP4 OCA].

1PP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP4 OCA].

==Reference==

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[[Category: gds(l) hydrolase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 23~~:59:~~22 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:02 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1pp4.gif|left|200px]]<br /><applet load="1pp4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pp4.gif|left|200px]]<br /><applet load="1pp4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pp4, resolution 2.5&Aring;" />
 '''The crystal structure of rhamnogalacturonan acetylesterase in space group P3121'''<br />
 ==Overview==
-The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus, aculeatus has been crystallized in two crystal forms, an orthorhombic and, a trigonal crystal form. In the orthorhombic crystal form, the covalently, bound carbohydrate at one of the two N-glycosylation sites is involved in, crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and, the trigonal crystal form at pH 4.5. In one case, the two crystal forms, were found in the same drop at pH 4.7. The differences in crystal packing, in the two crystal forms can be explained by the pH-dependent variation in, the protonation state of the glutamic acid residues on the protein, surface.
+The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface.
 ==About this Structure==
-PP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PP4 OCA].
+PP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP4 OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: gds(l) hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:59:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:02 2008''