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3thg

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Revision as of 16:58, 6 July 2022

Crystal structure of the creosote Rubisco activase C-domain

Structural highlights

3thg is a 1 chain structure with sequence from Creosote bush. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	RCA1 (Creosote bush)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RCA1_LARTR] Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.

Publication Abstract from PubMed

The rapid release of tight-binding inhibitors from dead-end ribulose-bisphosphate carboxylase/oxygenase (Rubisco) complexes requires the activity of Rubisco activase, an AAA+ ATPase that utilizes chemo-mechanical energy to catalyze the reactivation of Rubisco. Activase is thought to play a central role in coordinating the rate of CO(2) fixation with the light reactions of photosynthesis. Here, we present a 1.9 A crystal structure of the C-domain core of creosote activase. The fold consists of a canonical four-helix bundle, from which a paddle-like extension protrudes that entails a nine-turn helix lined by an irregularly structured peptide strand. The residues Lys-313 and Val-316 involved in the species-specific recognition of Rubisco are located near the tip of the paddle. An ionic bond between Lys-313 and Glu-309 appears to stabilize the glycine-rich end of the helix. Structural superpositions onto the distant homolog FtsH imply that the paddles extend away from the hexameric toroid in a fan-like fashion, such that the hydrophobic sides of each blade bearing Trp-302 are facing inward and the polar sides bearing Lys-313 and Val-316 are facing outward. Therefore, we speculate that upon binding, the activase paddles embrace the Rubisco cylinder by placing their hydrophobic patches near the partner protein. This model suggests that conformational adjustments at the remote end of the paddle may relate to selectivity in recognition, rather than specific ionic contacts involving Lys-313. Additionally, the superpositions predict that the catalytically critical Arg-293 does not interact with the bound nucleotide. Hypothetical ring-ring stacking and peptide threading models for Rubisco reactivation are briefly discussed.

Atomic resolution x-ray structure of the substrate recognition domain of higher plant ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase.,Henderson JN, Kuriata AM, Fromme R, Salvucci ME, Wachter RM J Biol Chem. 2011 Oct 14;286(41):35683-8. Epub 2011 Aug 31. PMID:21880724^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Henderson JN, Kuriata AM, Fromme R, Salvucci ME, Wachter RM. Atomic resolution x-ray structure of the substrate recognition domain of higher plant ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase. J Biol Chem. 2011 Oct 14;286(41):35683-8. Epub 2011 Aug 31. PMID:21880724 doi:10.1074/jbc.C111.289595

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3thg"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the creosote Rubisco activase C-domain==
-<StructureSection load='3thg' size='340' side='right' caption='[[3thg]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
+<StructureSection load='3thg' size='340' side='right'caption='[[3thg]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3thg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Creosote_bush Creosote bush]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3THG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3thg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Creosote_bush Creosote bush]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66636 Creosote bush])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66636 Creosote bush])</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=3thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thg OCA], [http://pdbe.org/3thg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3thg RCSB], [http://www.ebi.ac.uk/pdbsum/3thg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3thg ProSAT]</span></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=3thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thg OCA], [https://pdbe.org/3thg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thg RCSB], [https://www.ebi.ac.uk/pdbsum/3thg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RCA1_LARTR RCA1_LARTR]] Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
+[[https://www.uniprot.org/uniprot/RCA1_LARTR RCA1_LARTR]] Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[RuBisCO|RuBisCO]]
+*[[RuBisCO 3D structures|RuBisCO 3D structures]]
 == References ==
 <references/>
@@ Line 27: / Line 27: @@
 </StructureSection>
 [[Category: Creosote bush]]
+[[Category: Large Structures]]
 [[Category: Fromme, R]]
 [[Category: Henderson, J N]]

3thg

From Proteopedia

Revision as of 16:58, 6 July 2022

Crystal structure of the creosote Rubisco activase C-domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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