2v6a

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[[Image:2v6a.jpg|left|200px]]
[[Image:2v6a.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2v6a |SIZE=350|CAPTION= <scene name='initialview01'>2v6a</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2v6a", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+L'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2v6a| PDB=2v6a | SCENE= }}
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|RELATEDENTRY=[[1gk8|1GK8]], [[1uwa|1UWA]], [[1uw9|1UW9]], [[1uzh|1UZH]], [[1ir2|1IR2]], [[1uzd|1UZD]], [[2v63|2V63]], [[2v67|2V67]], [[2v68|2V68]], [[2v69|2V69]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6a OCA], [http://www.ebi.ac.uk/pdbsum/2v6a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v6a RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, G344S'''
'''CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, G344S'''
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[[Category: Spreitzer, R J.]]
[[Category: Spreitzer, R J.]]
[[Category: Taylor, T C.]]
[[Category: Taylor, T C.]]
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[[Category: acetylation]]
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[[Category: Acetylation]]
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[[Category: calvin cycle]]
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[[Category: Calvin cycle]]
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[[Category: carbon dioxide fixation]]
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[[Category: Carbon dioxide fixation]]
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[[Category: chloroplast]]
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[[Category: Chloroplast]]
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[[Category: co2/o2 specificity]]
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[[Category: Co2/o2 specificity]]
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[[Category: hydroxylation]]
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[[Category: Hydroxylation]]
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[[Category: large subunit loop 6 mutation]]
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[[Category: Large subunit loop 6 mutation]]
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[[Category: lyase]]
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[[Category: Lyase]]
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[[Category: magnesium]]
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[[Category: Magnesium]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: methylation]]
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[[Category: Methylation]]
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[[Category: monooxygenase]]
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[[Category: Monooxygenase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: photorespiration]]
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[[Category: Photorespiration]]
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[[Category: photosynthesis]]
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[[Category: Photosynthesis]]
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[[Category: plastid]]
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[[Category: Plastid]]
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[[Category: rubisco]]
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[[Category: Rubisco]]
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[[Category: transit peptide]]
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[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:15:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:47 2008''
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Revision as of 15:15, 4 May 2008

Template:STRUCTURE 2v6a

CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, G344S


Overview

The loop between alpha-helix 6 and beta-strand 6 in the alpha/beta-barrel of ribulose-1,5-bisphosphate carboxylase/oxygenase plays a key role in discriminating between CO2 and O2. Genetic screening in Chlamydomonas reinhardtii previously identified a loop-6 V331A substitution that decreases carboxylation and CO2/O2 specificity. Revertant selection identified T342I and G344S substitutions that restore photosynthetic growth by increasing carboxylation and specificity of the V331A enzyme. In numerous X-ray crystal structures, loop 6 is closed or open depending on the activation state of the enzyme and the presence or absence of ligands. The carboxy terminus folds over loop 6 in the closed state. To study the molecular basis for catalysis, directed mutagenesis and chloroplast transformation were used to create T342I and G344S substitutions alone. X-ray crystal structures were then solved for the V331A, V331A/T342I, T342I, and V331A/G344S enzymes, as well as for a D473E enzyme created to assess the role of the carboxy terminus in loop-6 closure. V331A disturbs a hydrophobic pocket, abolishing several van der Waals interactions. These changes are complemented by T342I and G344S, both of which alone cause decreases in CO2/O2 specificity. In the V331A/T342I revertant enzyme, Arg339 main-chain atoms are displaced. In V331A/G344S, alpha-helix 6 is shifted. D473E causes disorder of the carboxy terminus, but loop 6 remains closed. Interactions between a transition-state analogue and several residues are altered in the mutant enzymes. However, active-site Lys334 at the apex of loop 6 has a normal conformation. A variety of subtle interactions must be responsible for catalytic efficiency and CO2/O2 specificity.

About this Structure

2V6A is a Protein complex structure of sequences from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

Reference

Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase., Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I, Biochemistry. 2007 Oct 2;46(39):11080-9. Epub 2007 Sep 8. PMID:17824672 Page seeded by OCA on Sun May 4 18:15:56 2008

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