2dkb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2dkb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dkb, resolution 2.1&Aring;" /> '''DIALKYLGLYCINE DECARB...)
Line 1: Line 1:
-
[[Image:2dkb.jpg|left|200px]]<br /><applet load="2dkb" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2dkb.jpg|left|200px]]<br /><applet load="2dkb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2dkb, resolution 2.1&Aring;" />
caption="2dkb, resolution 2.1&Aring;" />
'''DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES'''<br />
'''DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES'''<br />
==Overview==
==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 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.
==About this Structure==
==About this Structure==
-
2DKB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia] with NA, PLP and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2,2-dialkylglycine_decarboxylase_(pyruvate) 2,2-dialkylglycine decarboxylase (pyruvate)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.64 4.1.1.64] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DKB OCA].
+
2DKB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2,2-dialkylglycine_decarboxylase_(pyruvate) 2,2-dialkylglycine decarboxylase (pyruvate)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.64 4.1.1.64] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DKB OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hohenester, E.]]
[[Category: Hohenester, E.]]
-
[[Category: Jansonius, J.N.]]
+
[[Category: Jansonius, J N.]]
-
[[Category: Toney, M.D.]]
+
[[Category: Toney, M D.]]
[[Category: MES]]
[[Category: MES]]
[[Category: NA]]
[[Category: NA]]
Line 22: Line 22:
[[Category: lyase(decarboxylase)]]
[[Category: lyase(decarboxylase)]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:38:26 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:59:52 2008''

Revision as of 14:59, 21 February 2008


2dkb, resolution 2.1Å

Drag the structure with the mouse to rotate

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.

About this Structure

2DKB is a Single protein structure of sequence from Burkholderia cepacia with , and as ligands. Active as 2,2-dialkylglycine decarboxylase (pyruvate), with EC number 4.1.1.64 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

Page seeded by OCA on Thu Feb 21 16:59:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools