6h7h: Difference between revisions
m Protected "6h7h" [edit=sysop:move=sysop] |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Crystal structure of redox-sensitive phosphoribulokinase (PRK) from Arabidopsis thaliana== | ||
<StructureSection load='6h7h' size='340' side='right'caption='[[6h7h]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6h7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H7H FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g32060, T12O21.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribulokinase Phosphoribulokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.19 2.7.1.19] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h7h OCA], [http://pdbe.org/6h7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h7h RCSB], [http://www.ebi.ac.uk/pdbsum/6h7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h7h ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In land plants and algae, the Calvin-Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga Chlamydomonas reinhardtii (CrPRK) and the land plant Arabidopsis thaliana (AtPRK). PRK is an elongated homodimer characterized by a large central beta-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 A apart and connected by a flexible region exclusive to photosynthetic eukaryotes-the clamp loop-which is believed to be essential for oxidation-induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both AtPRK and CrPRK have a strongly reduced dimer interface and an increased number of random-coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes. | |||
Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle.,Gurrieri L, Del Giudice A, Demitri N, Falini G, Pavel NV, Zaffagnini M, Polentarutti M, Crozet P, Marchand CH, Henri J, Trost P, Lemaire SD, Sparla F, Fermani S Proc Natl Acad Sci U S A. 2019 Mar 28. pii: 1820639116. doi:, 10.1073/pnas.1820639116. PMID:30923119<ref>PMID:30923119</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6h7h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arath]] | |||
[[Category: Large Structures]] | |||
[[Category: Phosphoribulokinase]] | |||
[[Category: Falini, G]] | |||
[[Category: Fermani, S]] | |||
[[Category: Gurrieri, L]] | [[Category: Gurrieri, L]] | ||
[[Category: Sparla, F]] | [[Category: Sparla, F]] | ||
[[Category: Trost, P]] | [[Category: Trost, P]] | ||
[[Category: | [[Category: Atp binding]] | ||
[[Category: | [[Category: Kinase]] | ||
[[Category: Photosynthesis]] | |||
[[Category: Transferase]] | |||
Latest revision as of 10:56, 24 April 2019
Crystal structure of redox-sensitive phosphoribulokinase (PRK) from Arabidopsis thalianaCrystal structure of redox-sensitive phosphoribulokinase (PRK) from Arabidopsis thaliana
Structural highlights
Publication Abstract from PubMedIn land plants and algae, the Calvin-Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga Chlamydomonas reinhardtii (CrPRK) and the land plant Arabidopsis thaliana (AtPRK). PRK is an elongated homodimer characterized by a large central beta-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 A apart and connected by a flexible region exclusive to photosynthetic eukaryotes-the clamp loop-which is believed to be essential for oxidation-induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both AtPRK and CrPRK have a strongly reduced dimer interface and an increased number of random-coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes. Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle.,Gurrieri L, Del Giudice A, Demitri N, Falini G, Pavel NV, Zaffagnini M, Polentarutti M, Crozet P, Marchand CH, Henri J, Trost P, Lemaire SD, Sparla F, Fermani S Proc Natl Acad Sci U S A. 2019 Mar 28. pii: 1820639116. doi:, 10.1073/pnas.1820639116. PMID:30923119[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||