2v6a
From Proteopedia
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|PDB= 2v6a |SIZE=350|CAPTION= <scene name='initialview01'>2v6a</scene>, resolution 1.50Å | |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> | |SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+L'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
| - | |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=[[1gk8|1GK8]], [[1uwa|1UWA]], [[1uw9|1UW9]], [[1uzh|1UZH]], [[1ir2|1IR2]], [[1uzd|1UZD]], [[2v63|2V63]], [[2v67|2V67]], [[2v68|2V68]], [[2v69|2V69]] | ||
| + | |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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[[Category: Spreitzer, R J.]] | [[Category: Spreitzer, R J.]] | ||
[[Category: Taylor, T C.]] | [[Category: Taylor, T C.]] | ||
| - | [[Category: CAP]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MG]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: calvin cycle]] | [[Category: calvin cycle]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:47 2008'' |
Revision as of 02:08, 31 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , , | ||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Related: | 1GK8, 1UWA, 1UW9, 1UZH, 1IR2, 1UZD, 2V63, 2V67, 2V68, 2V69
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 05:08:47 2008
Categories: Chlamydomonas reinhardtii | Protein complex | Ribulose-bisphosphate carboxylase | Andersson, I. | Karkehabadi, S. | Satagopan, S. | Spreitzer, R J. | Taylor, T C. | 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
