Glycoside Hydrolase Family 101 - Revision history

Harry Brumer: /* Three-dimensional structures */

2020-05-14T00:23:52Z

Three-dimensional structures

Harry Brumer at 02:41, 6 August 2013

2013-08-06T02:41:40Z

Harry Brumer: replaced missing Curator Approved stamp

2013-08-06T02:39:32Z

replaced missing Curator Approved stamp

Harry Brumer: updated CAZy DB link

2011-05-09T13:22:40Z

updated CAZy DB link

Harry Brumer at 16:18, 4 May 2011

2011-05-04T16:18:36Z

Harry Brumer: /* Three-dimensional structures */

2011-05-04T16:08:09Z

Three-dimensional structures

Harry Brumer: /* Three-dimensional structures */

2010-01-22T14:44:44Z

Three-dimensional structures

Warren Wakarchuk: /* Three-dimensional structures */

2009-12-11T21:45:34Z

Three-dimensional structures

Harry Brumer at 14:17, 8 November 2009

2009-11-08T14:17:01Z

Warren Wakarchuk: /* Catalytic Residues */

2009-10-23T13:51:10Z

Catalytic Residues

@@ Line 38: / Line 38: @@
 == Three-dimensional structures ==
 [[Image:Spgh101_all-domains_2.png|thumb|right|300px|'''Figure. SpGH101''' Legend.]]
-The recently solved 3D structure of SpGH101 reveals that this protein surprisingly shares some structural features with GH13 alpha-amylases, as well as containing potential carbohydrate binding modules.  In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel.  This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2A) than that of the SpGH101 (2.9A) <cite>7</cite>
+The recently solved 3D structure of SpGH101 reveals that this protein surprisingly shares some structural features with [[GH13]] alpha-amylases, as well as containing potential carbohydrate binding modules.  In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel.  This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2A) than that of the SpGH101 (2.9A) <cite>7</cite>
 == Family Firsts ==

@@ Line 37: / Line 37: @@
 == Three-dimensional structures ==
 The recently solved 3D structure of SpGH101 reveals that this protein surprisingly shares some structural features with GH13 alpha-amylases, as well as containing potential carbohydrate binding modules.  In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel.  This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2A) than that of the SpGH101 (2.9A) <cite>7</cite>
 == Family Firsts ==

← Older revision		Revision as of 02:39, 6 August 2013
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		+	{{CuratorApproved}}
	* [[Author]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]		* [[Author]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]
	* [[Responsible Curator]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]		* [[Responsible Curator]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]

@@ Line 1: / Line 1: @@
 * [[Author]]: [[User:WarrenWakarchuk|Warren Wakarchuk]]
 * [[Responsible Curator]]:  [[User:WarrenWakarchuk|Warren Wakarchuk]]
@@ Line 10: / Line 9: @@
 |-
 |'''Clan'''
-|none
+|GH-x
 |-
 |'''Mechanism'''
@@ Line 37: / Line 36: @@
 == Three-dimensional structures ==
-The recently solved 3D structure of SpGH101 reveals that this protein shares some structural features with [[GH13]] alpha-amylases, as well as containing potential carbohydrate binding modules.  In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel.  This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2 Å) than that of the SpGH101 (2.9 Å) <cite>7</cite>
+The recently solved 3D structure of SpGH101 reveals that this protein surprisingly shares some structural features with GH13 alpha-amylases, as well as containing potential carbohydrate binding modules.  In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel.  This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2A) than that of the SpGH101 (2.9A) <cite>7</cite>
-<gallery widths=400px heights=264px perrow=1 caption="SpGH101">
-File:Spgh101 all-domains 2.png
+[[Image:Spgh101_all-domains_2.png|SpGH101]]
 == Family Firsts ==

@@ Line 10: / Line 10: @@
 |-
 |'''Clan'''
-|GH-x
+|none
 |-
 |'''Mechanism'''
@@ Line 20: / Line 20: @@
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH101.html
+| colspan="2" |{{CAZyDBlink}}GH101.html
 |}
 </div>

← Older revision		Revision as of 21:45, 11 December 2009
Line 37:		Line 37:

	== Three-dimensional structures ==		== Three-dimensional structures ==
−	The recently solved 3D structure of SpGH101 reveals that this protein ~~surprisingly~~ shares some structural features with GH13 alpha-amylases, as well as containing potential carbohydrate binding modules. In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel. This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2A) than that of the SpGH101 (2.9A) <cite>7</cite>	+	The recently solved 3D structure of SpGH101 reveals that this protein shares some structural features with GH13 alpha-amylases, as well as containing potential carbohydrate binding modules. In the analysis of the 3D structure of SpGH101 the catalytic domain is a highly distorted (beta/alpha)<sub>8</sub> barrel. This barrel is flanked by a domain of all beta-sheet structure which is very analogous to the arrangement seen in GH13 alpha-amylase <cite>6</cite>. The BlGH101 enzyme was found to have an almost identical fold, although this structure was solved at higher resolution (2A) than that of the SpGH101 (2.9A) <cite>7</cite>

← Older revision		Revision as of 14:17, 8 November 2009
Line 1:		Line 1:
		+	{{CuratorApproved}}
	* [[Author]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]		* [[Author]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]
	* [[Responsible Curator]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]		* [[Responsible Curator]]: [[User:WarrenWakarchuk\|Warren Wakarchuk]]

@@ Line 32: / Line 32: @@
 == Catalytic Residues ==
-Using the enzyme from ''Streptococcus pneumoniae'' the [[catalytic nucleophile]] was determined as residue D764.  Willis ''et al.'' in preparation <cite>5</cite>
+Using the enzyme from ''Streptococcus pneumoniae'' the [[catalytic nucleophile]] was determined as residue D764.  Willis ''et al.'' <cite>5</cite>
 The [[general acid/base]] residue in SpGH101 was determined to be E796.