1bwv
From Proteopedia
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|PDB= 1bwv |SIZE=350|CAPTION= <scene name='initialview01'>1bwv</scene>, resolution 2.4Å | |PDB= 1bwv |SIZE=350|CAPTION= <scene name='initialview01'>1bwv</scene>, resolution 2.4Å | ||
|SITE= <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> | |SITE= <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> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwv OCA], [http://www.ebi.ac.uk/pdbsum/1bwv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bwv RCSB]</span> | ||
}} | }} | ||
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[[Category: Yamamoto, H.]] | [[Category: Yamamoto, H.]] | ||
[[Category: Yokota, A.]] | [[Category: Yokota, A.]] | ||
| - | + | [[Category: carbon dioxide fixation,complex (rubisco/reaction intermediate)]] | |
| - | + | ||
| - | [[Category: carbon dioxide fixation | + | |
| - | + | ||
[[Category: high specificity factor]] | [[Category: high specificity factor]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:10:00 2008'' |
Revision as of 16:10, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 19:10:00 2008
