We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1bwv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bwv.gif|left|200px]]<br />
+
[[Image:1bwv.jpg|left|200px]]<br /><applet load="1bwv" size="450" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1bwv" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1bwv, resolution 2.4&Aring;" />
caption="1bwv, resolution 2.4&Aring;" />
'''ACTIVATED RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH THE REACTION INTERMEDIATE ANALOGUE 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE'''<br />
'''ACTIVATED RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH THE REACTION INTERMEDIATE ANALOGUE 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE'''<br />
Line 8: Line 7:
==About this Structure==
==About this Structure==
-
1BWV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita] with MG and CAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] Structure known Active Sites: MGA, MGC, MGE and MGG. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BWV OCA].
+
1BWV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita] with MG and CAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] Known structural/functional Sites: <scene name='pdbsite=MGA:Mg Binding Site Chain A'>MGA</scene>, <scene name='pdbsite=MGC:Mg Binding Site Chain C'>MGC</scene>, <scene name='pdbsite=MGE:Mg Binding Site Chain E'>MGE</scene> and <scene name='pdbsite=MGG:Mg Binding Site Chain G'>MGG</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BWV OCA].
==Reference==
==Reference==
Line 29: Line 28:
[[Category: lyase]]
[[Category: lyase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:57:47 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:35:11 2007''

Revision as of 12:25, 18 December 2007


1bwv, resolution 2.4Å

Drag the structure with the mouse to rotate

ACTIVATED RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH THE REACTION INTERMEDIATE ANALOGUE 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE

Overview

We determined the crystal structure of spinach ribulose-1, 5-bisphosphate, carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution, and found that the enzyme contained two kinds of S, SI and SII, present in, equal number and disposed in an orderly way within the Rubisco holoenzyme., The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue, differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The, orderly disposition of the heterogeneous small subunits in the Rubisco, holoenzyme provides accounts of a multigene family of S in plants.

About this Structure

1BWV is a Protein complex structure of sequences from Galdieria partita with MG and CAP as ligands. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

Reference

Orderly disposition of heterogeneous small subunits in D-ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach., Shibata N, Inoue T, Fukuhara K, Nagara Y, Kitagawa R, Harada S, Kasai N, Uemura K, Kato K, Yokota A, Kai Y, J Biol Chem. 1996 Oct 25;271(43):26449-52. PMID:8900108

Page seeded by OCA on Tue Dec 18 14:35:11 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools