2dkb: Difference between revisions

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[[Image:2dkb.~~jpg~~|left|200px]]

[[Image:2dkb.png|left|200px]]

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~~'''~~DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES~~'''~~

===DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES===

~~==Overview==~~

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The ~~structure of~~ the ~~bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined~~ to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the ~~active site and accounts for the dependence of activity~~ on ~~potassium ions~~. ~~The other~~ is ~~located at~~ the ~~carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects~~.

The line below this paragraph, {{ABSTRACT_PUBMED_8342040}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8342040 is the PubMed ID number.

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==About this Structure==

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[[Category: Jansonius, J N.]]

[[Category: Toney, M D.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 00~~:36:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:51:41 2008''

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-[[Image:2dkb.jpg|left|200px]]
+{{Seed}}
+[[Image:2dkb.png|left|200px]]
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 {{STRUCTURE_2dkb|  PDB=2dkb  |  SCENE=  }}
-'''DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES'''
+===DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES===
-==Overview==
+<!--
-The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.
+The line below this paragraph, {{ABSTRACT_PUBMED_8342040}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8342040 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8342040}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Jansonius, J N.]]
 [[Category: Toney, M D.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:36:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:51:41 2008''