6hzk
From Proteopedia
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<StructureSection load='6hzk' size='340' side='right'caption='[[6hzk]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='6hzk' size='340' side='right'caption='[[6hzk]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6hzk]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6hzk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HZK FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzk OCA], [https://pdbe.org/6hzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hzk RCSB], [https://www.ebi.ac.uk/pdbsum/6hzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzk ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0H3K6J7_SYNP6 A0A0H3K6J7_SYNP6] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phosphoribulokinase (PRK) catalyses the ATP-dependent phosphorylation of ribulose 5-phosphate to give ribulose 1,5-bisphosphate. Regulation of this reaction in response to light controls carbon fixation during photosynthesis. Here, the crystal structure of PRK from the cyanobacterium Synechococcus sp. strain PCC 6301 is presented. The enzyme is dimeric and has an alpha/beta-fold with an 18-stranded beta-sheet at its core. Interestingly, a disulfide bond is found between Cys40 and the P-loop residue Cys18, revealing the structural basis for the redox inactivation of PRK activity. A second disulfide bond appears to rigidify the dimer interface and may thereby contribute to regulation by the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase. | ||
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| + | Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301.,Wilson RH, Hayer-Hartl M, Bracher A Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):278-289. doi:, 10.1107/S2053230X19002693. Epub 2019 Apr 2. PMID:30950829<ref>PMID:30950829</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6hzk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Anacystis nidulans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Synechococcus elongatus PCC 6301]] |
| - | [[Category: Bracher | + | [[Category: Bracher A]] |
| - | [[Category: Hartl | + | [[Category: Hartl FU]] |
| - | [[Category: Hayer-Hartl | + | [[Category: Hayer-Hartl M]] |
| - | [[Category: Wilson | + | [[Category: Wilson RH]] |
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Current revision
Crystal structure of redox-inhibited phosphoribulokinase from Synechococcus sp. (strain PCC 6301)
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