2v6a
From Proteopedia
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| - | [[Image:2v6a.jpg|left|200px]] | + | [[Image:2v6a.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, G344S''' | + | {{Structure |
| + | |PDB= 2v6a |SIZE=350|CAPTION= <scene name='initialview01'>2v6a</scene>, resolution 1.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+L'>AC1</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=EDO:1,2-ETHANEDIOL'>EDO</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= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, G344S''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V6A is a [ | + | 2V6A is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6A OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17824672 17824672] |
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:33 2008'' |
Revision as of 16:43, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 18:43:33 2008
Categories: Chlamydomonas reinhardtii | Protein complex | Ribulose-bisphosphate carboxylase | Andersson, I. | Karkehabadi, S. | Satagopan, S. | Spreitzer, R J. | Taylor, T C. | CAP | EDO | MG | Acetylation | Calvin cycle | Carbon dioxide fixation | Chloroplast | Co2/o2 specificity | Hydroxylation | Large subunit loop 6 mutation | Lyase | Magnesium | Metal-binding | Methylation | Monooxygenase | Oxidoreductase | Photorespiration | Photosynthesis | Plastid | Rubisco | Transit peptide
