1rbl: Difference between revisions

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[[Image:1rbl.gif|left|200px]]<br /><applet load="1rbl" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1rbl.gif|left|200px]]
caption="1rbl, resolution 2.2&Aring;" />
 
'''STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301'''<br />
{{Structure
|PDB= 1rbl |SIZE=350|CAPTION= <scene name='initialview01'>1rbl</scene>, resolution 2.2&Aring;
|SITE= <scene name='pdbsite=1:Site_identifier+Cab'>1</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</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]
|GENE=
}}
 
'''STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1RBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CAP:'>CAP</scene> and <scene name='pdbligand=FMT:'>FMT</scene> 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 Site: <scene name='pdbsite=1:Site_identifier+Cab'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RBL OCA].  
1RBL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RBL OCA].  


==Reference==
==Reference==
Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301., Newman J, Branden CI, Jones TA, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):548-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299492 15299492]
Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301., Newman J, Branden CI, Jones TA, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):548-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299492 15299492]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Ribulose-bisphosphate carboxylase]]
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[[Category: lyase(carbon-carbon)]]
[[Category: lyase(carbon-carbon)]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:09 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:49:29 2008''

Revision as of 11:49, 20 March 2008

File:1rbl.gif


Drag the structure with the mouse to rotate
1rbl, resolution 2.2Å
Sites: 1
Ligands: MG, CAP and FMT
Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Coordinates: save as pdb, mmCIF, xml



STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301


Overview

The structure of an activated quaternary complex of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus PCC6301 has been solved by molecular replacement. The protein crystallizes in an orthorhombic P2(1)2(1)2(1) unit cell with a complete L(8)S(8) complex consisting of 4608 residues (37 680 non-hydrogen atoms) in the asymmetric unit. Data were collected both on film and image plate using synchrotron radiation; there were 218 276 unique reflections in the final 2.2 A data set. The eightfold non-crystallographic symmetry could be used both to improve map quality and to reduce the computing requirements of refinement. The coordinates were refined using strict non-crystallographic symmetry constraints. The stereochemistry of the final model is good, and the model has an R value of 20.0% for the reflections between 7 and 2.2 A.

About this Structure

1RBL is a Protein complex structure of sequences from Synechococcus sp.. Full crystallographic information is available from OCA.

Reference

Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301., Newman J, Branden CI, Jones TA, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):548-60. PMID:15299492

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