1znn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1znn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1znn, resolution 2.20&Aring;" /> '''Structure of the syn...)
Line 1: Line 1:
-
[[Image:1znn.gif|left|200px]]<br /><applet load="1znn" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1znn.gif|left|200px]]<br /><applet load="1znn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1znn, resolution 2.20&Aring;" />
caption="1znn, resolution 2.20&Aring;" />
'''Structure of the synthase subunit of PLP synthase'''<br />
'''Structure of the synthase subunit of PLP synthase'''<br />
==Overview==
==Overview==
-
Pyridoxal 5'-phosphate (PLP, vitamin B6), a cofactor in many enzymatic, reactions, has two distinct biosynthetic routes, which do not coexist in, any organism. Two proteins, known as PdxS and PdxT, together form a PLP, synthase in plants, fungi, archaea, and some eubacteria. PLP synthase is a, heteromeric glutamine amidotransferase in which PdxT produces ammonia from, glutamine and PdxS combines ammonia with five- and three-carbon, phosphosugars to form PLP. In the 2.2-A crystal structure, PdxS is a, cylindrical dodecamer of subunits having the classic (beta/alpha)8 barrel, fold. PdxS subunits form two hexameric rings with the active sites, positioned on the inside. The hexamer and dodecamer forms coexist in, solution. A novel phosphate-binding site is suggested by bound sulfate., The sulfate and another bound molecule, methyl pentanediol, were used to, model the substrate ribulose 5-phosphate, and to propose catalytic roles, for residues in the active site. The distribution of conserved surfaces in, the PdxS dodecamer was used to predict a docking site for the glutaminase, partner, PdxT.
+
Pyridoxal 5'-phosphate (PLP, vitamin B6), a cofactor in many enzymatic reactions, has two distinct biosynthetic routes, which do not coexist in any organism. Two proteins, known as PdxS and PdxT, together form a PLP synthase in plants, fungi, archaea, and some eubacteria. PLP synthase is a heteromeric glutamine amidotransferase in which PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. In the 2.2-A crystal structure, PdxS is a cylindrical dodecamer of subunits having the classic (beta/alpha)8 barrel fold. PdxS subunits form two hexameric rings with the active sites positioned on the inside. The hexamer and dodecamer forms coexist in solution. A novel phosphate-binding site is suggested by bound sulfate. The sulfate and another bound molecule, methyl pentanediol, were used to model the substrate ribulose 5-phosphate, and to propose catalytic roles for residues in the active site. The distribution of conserved surfaces in the PdxS dodecamer was used to predict a docking site for the glutaminase partner, PdxT.
==About this Structure==
==About this Structure==
-
1ZNN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with SO4 and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZNN OCA].
+
1ZNN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNN OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Belitsky, B.R.]]
+
[[Category: Belitsky, B R.]]
-
[[Category: Burgner, J.W.]]
+
[[Category: Burgner, J W.]]
[[Category: Harms, E.]]
[[Category: Harms, E.]]
-
[[Category: Smith, J.L.]]
+
[[Category: Smith, J L.]]
[[Category: Zhu, J.]]
[[Category: Zhu, J.]]
[[Category: MRD]]
[[Category: MRD]]
Line 22: Line 22:
[[Category: tim barrel]]
[[Category: tim barrel]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:33:28 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:21 2008''

Revision as of 14:17, 21 February 2008


1znn, resolution 2.20Å

Drag the structure with the mouse to rotate

Structure of the synthase subunit of PLP synthase

Overview

Pyridoxal 5'-phosphate (PLP, vitamin B6), a cofactor in many enzymatic reactions, has two distinct biosynthetic routes, which do not coexist in any organism. Two proteins, known as PdxS and PdxT, together form a PLP synthase in plants, fungi, archaea, and some eubacteria. PLP synthase is a heteromeric glutamine amidotransferase in which PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. In the 2.2-A crystal structure, PdxS is a cylindrical dodecamer of subunits having the classic (beta/alpha)8 barrel fold. PdxS subunits form two hexameric rings with the active sites positioned on the inside. The hexamer and dodecamer forms coexist in solution. A novel phosphate-binding site is suggested by bound sulfate. The sulfate and another bound molecule, methyl pentanediol, were used to model the substrate ribulose 5-phosphate, and to propose catalytic roles for residues in the active site. The distribution of conserved surfaces in the PdxS dodecamer was used to predict a docking site for the glutaminase partner, PdxT.

About this Structure

1ZNN is a Protein complex structure of sequences from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.

Reference

A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase., Zhu J, Burgner JW, Harms E, Belitsky BR, Smith JL, J Biol Chem. 2005 Jul 29;280(30):27914-23. Epub 2005 May 23. PMID:15911615

Page seeded by OCA on Thu Feb 21 16:17:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools