3syl: Difference between revisions

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'''Unreleased structure'''


The entry 3syl is ON HOLD  until Paper Publication
==Crystal structure of the AAA+ protein CbbX, native structure==
 
<StructureSection load='3syl' size='340' side='right'caption='[[3syl]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
Authors: Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F.U., Bracher, A., Hayer-Hartl, M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3syl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SYL FirstGlance]. <br>
Description: Crystal structure of the AAA+ protein CbbX, native structure
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3syl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3syl OCA], [https://pdbe.org/3syl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3syl RCSB], [https://www.ebi.ac.uk/pdbsum/3syl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3syl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBBX_CERSP CBBX_CERSP] ATPase involved in the activation of red-type RuBisCo (ribulose-1,5-bisphosphate carboxylase/oxygenase), which tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP) (PubMed:27872295, PubMed:22048315). Catalyzes the release of RuBP from inhibited RuBisCo in an ATP-dependent manner (PubMed:27872295, PubMed:22048315). Activation of RuBisCO involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure (PubMed:27872295, PubMed:22048315).<ref>PMID:22048315</ref> <ref>PMID:27872295</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cereibacter sphaeroides]]
[[Category: Large Structures]]
[[Category: Bracher A]]
[[Category: Hartl FU]]
[[Category: Hayer-Hartl M]]
[[Category: Mueller-Cajar O]]
[[Category: Stotz M]]
[[Category: Wendler P]]

Latest revision as of 16:12, 14 March 2024

Crystal structure of the AAA+ protein CbbX, native structureCrystal structure of the AAA+ protein CbbX, native structure

Structural highlights

3syl is a 2 chain structure with sequence from Cereibacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBBX_CERSP ATPase involved in the activation of red-type RuBisCo (ribulose-1,5-bisphosphate carboxylase/oxygenase), which tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP) (PubMed:27872295, PubMed:22048315). Catalyzes the release of RuBP from inhibited RuBisCo in an ATP-dependent manner (PubMed:27872295, PubMed:22048315). Activation of RuBisCO involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure (PubMed:27872295, PubMed:22048315).[1] [2]

References

  1. Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature. 2011 Nov 2;479(7372):194-9. doi: 10.1038/nature10568. PMID:22048315 doi:10.1038/nature10568
  2. Loganathan N, Tsai YC, Mueller-Cajar O. Characterization of the heterooligomeric red-type rubisco activase from red algae. Proc Natl Acad Sci U S A. 2016 Dec 6;113(49):14019-14024. PMID:27872295 doi:10.1073/pnas.1610758113

3syl, resolution 3.00Å

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