5bq1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BQ1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BQ1 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</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]] 1.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5bq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bq1 OCA], [https://pdbe.org/5bq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bq1 RCSB], [https://www.ebi.ac.uk/pdbsum/5bq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bq1 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=5bq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bq1 OCA], [https://pdbe.org/5bq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bq1 RCSB], [https://www.ebi.ac.uk/pdbsum/5bq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bq1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9HVB9_PSEAE Q9HVB9_PSEAE] | [https://www.uniprot.org/uniprot/Q9HVB9_PSEAE Q9HVB9_PSEAE] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM approximately 10(8) M(-1) s(-1)). This family of enzymes has evolved disparate protein folds that all perform the same reaction at near catalytic perfection. Presented here is a structural study of a beta-CA (psCA3) expressed in Pseudomonas aeruginosa, in complex with CO2, using pressurized cryo-cooled crystallography. The structure has been refined to 1.6 A resolution with Rcryst and Rfree values of 17.3 and 19.9%, respectively, and is compared with the alpha-CA, human CA isoform II (hCA II), the only other CA to have CO2 captured in its active site. Despite the lack of structural similarity between psCA3 and hCA II, the CO2 binding orientation relative to the zinc-bound solvent is identical. In addition, a second CO2 binding site was located at the dimer interface of psCA3. Interestingly, all beta-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions. | ||
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| - | Carbon Dioxide "Trapped" in a beta-Carbonic Anhydrase.,Aggarwal M, Chua TK, Pinard MA, Szebenyi DM, McKenna R Biochemistry. 2015 Nov 3;54(43):6631-8. doi: 10.1021/acs.biochem.5b00987. Epub, 2015 Oct 16. PMID:26457866<ref>PMID:26457866</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5bq1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Capturing Carbon Dioxide in beta Carbonic Anhydrase
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