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| - | [[Image:1bxn.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bxn| PDB=1bxn | SCENE= }} | | {{STRUCTURE_1bxn| PDB=1bxn | SCENE= }} |
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| - | '''THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7 ANGSTROMS.'''
| + | ===THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7 ANGSTROMS.=== |
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| - | ==Overview==
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| - | Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is involved in photosynthesis where it catalyzes the initial step in the fixation of carbon dioxide. The enzyme also catalyzes a competing oxygenation reaction leading to loss of fixed carbon dioxide, thus reducing the net efficiency of photosynthesis significantly. Rubisco has therefore been studied extensively, and a challenging goal is the engineering of a more photosynthetically efficient enzyme. Hexadecameric rubiscos fall in two distinct groups, "green-like" and "red-like". The ability to discriminate between CO2 and O2 as substrates varies significantly, and some algae have red-like rubisco with even higher specificity for CO2 than the plant enzyme. The structure of unactivated rubisco from Alcaligenes eutrophus has been determined to 2.7 A resolution by molecular replacement and refined to R and Rfree values of 26.6 and 32.2 %, respectively. The overall fold of the protein is very similar to the rubisco structures solved previously for green-like hexadecameric enzymes, except for the extended C-terminal domains of the small subunits which together form an eight-stranded beta-barrel which sits as a plug in the entrance to the central solvent channel in the molecule. The present structure is the first which has been solved for a red-like rubisco and is likely to represent a fold which is common for this group. The small subunits in general are believed to have a stabilizing effect, and the new quaternary structure in the oligomer of the present structure is likely to contribute even more to this stabilization of the assembled rubisco protein.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10329167}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10329167 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10329167}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hough, E.]] | | [[Category: Hough, E.]] |
| | [[Category: Vollan, V B.]] | | [[Category: Vollan, V B.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:05:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:52:54 2008'' |
Revision as of 16:52, 30 June 2008
Template:STRUCTURE 1bxn
THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7 ANGSTROMS.
Template:ABSTRACT PUBMED 10329167
About this Structure
1BXN is a Protein complex structure of sequences from Cupriavidus necator. Full crystallographic information is available from OCA.
Reference
The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits., Hansen S, Vollan VB, Hough E, Andersen K, J Mol Biol. 1999 May 14;288(4):609-21. PMID:10329167
Page seeded by OCA on Mon Jun 30 19:52:54 2008
