1dka: Difference between revisions

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[[Image:1dka.jpg|left|200px]]
{{Seed}}
[[Image:1dka.png|left|200px]]


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{{STRUCTURE_1dka|  PDB=1dka  |  SCENE=  }}  
{{STRUCTURE_1dka|  PDB=1dka  |  SCENE=  }}  


'''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.
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{{ABSTRACT_PUBMED_8342040}}


==About this Structure==
==About this Structure==
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[[Category: Jansonius, J N.]]
[[Category: Jansonius, J N.]]
[[Category: Toney, M D.]]
[[Category: Toney, M D.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:56:53 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:12:02 2008''

Revision as of 20:12, 30 June 2008

File:1dka.png

Template:STRUCTURE 1dka

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

Template:ABSTRACT PUBMED 8342040

About this Structure

1DKA is a Single protein structure of sequence from Burkholderia cepacia. Full crystallographic information is available from OCA.

Reference

Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites., Toney MD, Hohenester E, Cowan SW, Jansonius JN, Science. 1993 Aug 6;261(5122):756-9. PMID:8342040

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