1yq2: Difference between revisions

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[[Image:1yq2.gif|left|200px]]<br /><applet load="1yq2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1yq2.gif|left|200px]]<br /><applet load="1yq2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1yq2, resolution 1.90Å" />

'''beta-galactosidase from Arthrobacter sp. C2-2 (isoenzyme C2-2-1)'''<br />

==Overview==

The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1), from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A, resolution. The enzyme forms 660 kDa hexamers with active sites opened to, the central cavity of the hexamer and connected by eight channels with, exterior solvent. To our best knowledge, this is the first cold-active, beta-galactosidase with known structure and also the first known, beta-galactosidase structure in the form of compact hexamers. The hexamer, organization regulates access of substrates and ligands to six active, sites and this unique packing, present also in solution, raises questions, about its purpose and function. This enzyme belongs to glycosyl hydrolase, family 2, similarly to Escherichia coli beta-galactosidase, forming, tetramers necessary for its enzymatic function. However, we discovered, significant differences between these two enzymes affecting the ability of, tetramer/hexamer formation and complementation of the active site. This, structure reveals new insights into the cold-adaptation mechanisms of, enzymatic pathways of extremophiles.

The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1) from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A resolution. The enzyme forms 660 kDa hexamers with active sites opened to the central cavity of the hexamer and connected by eight channels with exterior solvent. To our best knowledge, this is the first cold-active beta-galactosidase with known structure and also the first known beta-galactosidase structure in the form of compact hexamers. The hexamer organization regulates access of substrates and ligands to six active sites and this unique packing, present also in solution, raises questions about its purpose and function. This enzyme belongs to glycosyl hydrolase family 2, similarly to Escherichia coli beta-galactosidase, forming tetramers necessary for its enzymatic function. However, we discovered significant differences between these two enzymes affecting the ability of tetramer/hexamer formation and complementation of the active site. This structure reveals new insights into the cold-adaptation mechanisms of enzymatic pathways of extremophiles.

==About this Structure==

1YQ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._1264c Arthrobacter sp. 1264c] with MG, NA, CL, SO4 and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YQ2 OCA].

1YQ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._1264c Arthrobacter sp. 1264c] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQ2 OCA].

==Reference==

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[[Category: glycosyl hydrolase family 2; tim barrel; hexamer]]

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@@ Line 1: / Line 1: @@
-[[Image:1yq2.gif|left|200px]]<br /><applet load="1yq2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1yq2.gif|left|200px]]<br /><applet load="1yq2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1yq2, resolution 1.90&Aring;" />
 '''beta-galactosidase from Arthrobacter sp. C2-2 (isoenzyme C2-2-1)'''<br />
 ==Overview==
-The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1), from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A, resolution. The enzyme forms 660 kDa hexamers with active sites opened to, the central cavity of the hexamer and connected by eight channels with, exterior solvent. To our best knowledge, this is the first cold-active, beta-galactosidase with known structure and also the first known, beta-galactosidase structure in the form of compact hexamers. The hexamer, organization regulates access of substrates and ligands to six active, sites and this unique packing, present also in solution, raises questions, about its purpose and function. This enzyme belongs to glycosyl hydrolase, family 2, similarly to Escherichia coli beta-galactosidase, forming, tetramers necessary for its enzymatic function. However, we discovered, significant differences between these two enzymes affecting the ability of, tetramer/hexamer formation and complementation of the active site. This, structure reveals new insights into the cold-adaptation mechanisms of, enzymatic pathways of extremophiles.
+The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1) from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A resolution. The enzyme forms 660 kDa hexamers with active sites opened to the central cavity of the hexamer and connected by eight channels with exterior solvent. To our best knowledge, this is the first cold-active beta-galactosidase with known structure and also the first known beta-galactosidase structure in the form of compact hexamers. The hexamer organization regulates access of substrates and ligands to six active sites and this unique packing, present also in solution, raises questions about its purpose and function. This enzyme belongs to glycosyl hydrolase family 2, similarly to Escherichia coli beta-galactosidase, forming tetramers necessary for its enzymatic function. However, we discovered significant differences between these two enzymes affecting the ability of tetramer/hexamer formation and complementation of the active site. This structure reveals new insights into the cold-adaptation mechanisms of enzymatic pathways of extremophiles.
 ==About this Structure==
-YQ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._1264c Arthrobacter sp. 1264c] with MG, NA, CL, SO4 and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YQ2 OCA].
+YQ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._1264c Arthrobacter sp. 1264c] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQ2 OCA].
 ==Reference==
@@ Line 30: / Line 30: @@
 [[Category: glycosyl hydrolase family 2; tim barrel; hexamer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:28:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:53 2008''