2nv0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2nv0.gif|left|200px]]
[[Image:2nv0.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2nv0 |SIZE=350|CAPTION= <scene name='initialview01'>2nv0</scene>, resolution 1.73&Aring;
+
The line below this paragraph, containing "STRUCTURE_2nv0", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= pdxT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2nv0| PDB=2nv0 | SCENE= }}
-
|RELATEDENTRY=[[1r9g|1R9G]], [[2nv1|2NV1]], [[2nv2|2NV2]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nv0 OCA], [http://www.ebi.ac.uk/pdbsum/2nv0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nv0 RCSB]</span>
+
-
}}
+
'''Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis'''
'''Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis'''
Line 28: Line 25:
[[Category: Strohmeier, M.]]
[[Category: Strohmeier, M.]]
[[Category: Tews, I.]]
[[Category: Tews, I.]]
-
[[Category: 3-layer(aba) sandwich]]
+
[[Category: Glutaminase]]
-
[[Category: glutaminase]]
+
[[Category: Rossmann fold]]
-
[[Category: rossmann fold]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:56:30 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:48 2008''
+

Revision as of 06:56, 4 May 2008

Template:STRUCTURE 2nv0

Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis


Overview

Vitamin B6 is an essential metabolic cofactor that has more functions in humans than any other single nutrient. Its de novo biosynthesis occurs through two mutually exclusive pathways that are absent in animals. The predominant pathway found in most prokaryotes, fungi, and plants has only recently been discovered. It is distinguished by a glutamine amidotransferase, which is remarkable in that it alone can synthesize the cofactor form, pyridoxal 5'-phosphate (PLP), directly from a triose and a pentose saccharide and glutamine. Here we report the 3D structure of the PLP synthase complex with substrate glutamine bound as well as those of the individual synthase and glutaminase subunits Pdx1 and Pdx2, respectively. The complex is made up of 24 protein units assembled like a cogwheel, a dodecameric Pdx1 to which 12 Pdx2 subunits attach. In contrast to the architecture of previously determined glutamine amidotransferases, macromolecular assembly is directed by an N-terminal alpha-helix on the synthase. Interaction with the synthase subunit leads to glutaminase activation, resulting in formation of an oxyanion hole, a prerequisite for catalysis. Mutagenesis permitted identification of the remote glutaminase and synthase catalytic centers and led us to propose a mechanism whereby ammonia shuttles between these active sites through a methionine-rich hydrophobic tunnel.

About this Structure

2NV0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structure of a bacterial pyridoxal 5'-phosphate synthase complex., Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I, Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19284-9. Epub 2006 Dec 11. PMID:17159152 Page seeded by OCA on Sun May 4 09:56:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools