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| | <StructureSection load='5swc' size='340' side='right'caption='[[5swc]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='5swc' size='340' side='right'caption='[[5swc]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5swc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SWC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5swc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SWC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">icfA, slr1347 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=5swc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5swc OCA], [https://pdbe.org/5swc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5swc RCSB], [https://www.ebi.ac.uk/pdbsum/5swc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5swc ProSAT]</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=5swc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5swc OCA], [http://pdbe.org/5swc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5swc RCSB], [http://www.ebi.ac.uk/pdbsum/5swc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5swc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYNT_SYNY3 CYNT_SYNY3]] Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation. | + | [https://www.uniprot.org/uniprot/CYNT_SYNY3 CYNT_SYNY3] Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carbonate dehydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Syny3]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Kimber MS]] |
| - | [[Category: McGurn, L]] | + | [[Category: McGurn L]] |
| - | [[Category: White, S A]] | + | [[Category: White SA]] |
| - | [[Category: Bacterial microcompartment]]
| + | |
| - | [[Category: Carbon fixation]]
| + | |
| - | [[Category: Carbonic anhydrase]]
| + | |
| - | [[Category: Carboxysome]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Symmetry breaking]]
| + | |
| Structural highlights
Function
CYNT_SYNY3 Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation.
Publication Abstract from PubMed
CcaA is a b-carbonic anhydrase that is a component of the carboxysomes of a subset of b-cyanobacteria. This protein, which has a characteristic C-terminal extension of unknown function, is recruited to the carboxysome via interactions with CcmM, which is itself a gamma-carbonic anhydrase homolog with enzymatic activity in many, but not all cyanobacteria. We have determined the structure of CcaA from Synechocystis sp. PCC 6803 at 1.45 A. In contrast to the dimer of dimers organization of most bacterial beta-carbonic anhydrases, or the loose dimer-of-dimers-of-dimers organization found in the plant enzymes, CcaA shows a well-packed trimer-of-dimers organization. The proximal part of the characteristic C-terminal extension is ordered by binding at a site that passes through the two-fold symmetry axis shared with an adjacent dimer; as a result, only one of a pair of converging termini can be ordered at any given time. Docking in Rosetta failed to find well-packed solutions, indicating that formation of the CcaA / CcmM complex likely requires significant backbone movements in at least one of the binding partners. Surface plasmon resonance experiments showed that CcaA forms a complex with CcmM with sub-picomolar affinity, with contributions from residues in CcmM's alphaA helix, and CcaA's C-terminal tail. Catalytic characterization showed CcaA to be among the least active beta-carbonic anhydrases characterized to date, with activity comparable to the gamma-carbonic anhydrase, CcmM, it either complements or replaces. Intriguingly, the C-terminal tail appears to partly inhibit activity, possibly indicating a role in minimizing the activity of unencapsulated enzyme.
The structure, kinetics and interactions of the beta-carboxysomal beta-carbonic anhydrase, CcaA.,McGurn LD, Moazami-Goudarzi M, White SA, Suwal T, Brar B, Tang JQ, Espie GS, Kimber MS Biochem J. 2016 Oct 11. pii: BCJ20160773. PMID:27729545[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McGurn LD, Moazami-Goudarzi M, White SA, Suwal T, Brar B, Tang JQ, Espie GS, Kimber MS. The structure, kinetics and interactions of the beta-carboxysomal beta-carbonic anhydrase, CcaA. Biochem J. 2016 Oct 11. pii: BCJ20160773. PMID:27729545 doi:http://dx.doi.org/10.1042/BCJ20160773
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