3b1b: Difference between revisions
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The | ==The unique structure of wild type carbonic anhydrase alpha-CA1 from Chlamydomonas reinhardtii== | ||
<StructureSection load='3b1b' size='340' side='right'caption='[[3b1b]], [[Resolution|resolution]] 1.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3b1b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B1B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3b1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b1b OCA], [https://pdbe.org/3b1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b1b RCSB], [https://www.ebi.ac.uk/pdbsum/3b1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b1b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAH1_CHLRE CAH1_CHLRE] Reversible hydration of carbon dioxide. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chlamydomonas reinhardtii alpha-type carbonic anhydrase (Cr-alphaCA1) is a dimeric enzyme that catalyses the interconversion of carbon dioxide and carbonic acid. The precursor form of Cr-alphaCA1 undergoes post-translational cleavage and N-glycosylation. Comparison of the genomic sequences of precursor Cr-alphaCA1 and other alphaCAs shows that Cr-alphaCA1 contains a different N-terminal sequence and two insertion sequences. A 35-residue peptide in one of the insertion sequences is deleted from the precursor during maturation. The crystal structure of the mature form of Cr-alphaCA1 has been determined at 1.88 A resolution. Each subunit is cleaved into the long and short peptides, but they are linked together by a disulfide bond. The two subunits are linked by a disulfide bond. N-Glycosylations occur at three asparagine residues and the attached N-glycans protrude into solvent regions. The subunits consist of a core beta-sheet structure composed of nine beta-strands. At the centre of the beta-sheet is the catalytic site, which contains a Zn atom bound to three histidine residues. The amino-acid residues around the Zn atom are highly conserved in other monomeric and dimeric alphaCAs. The short peptide runs near the active site and forms a hydrogen bond to the zinc-coordinated residue in the long chain, suggesting an important role for the short peptide in Cr-alphaCA1 activity. | |||
The unique structure of carbonic anhydrase alphaCA1 from Chlamydomonas reinhardtii.,Suzuki K, Yang SY, Shimizu S, Morishita EC, Jiang J, Zhang F, Hoque MM, Sato Y, Tsunoda M, Sekiguchi T, Takenaka A Acta Crystallogr D Biol Crystallogr. 2011 Oct;67(Pt 10):894-901. Epub 2011 Sep 8. PMID:21931221<ref>PMID:21931221</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3b1b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chlamydomonas reinhardtii]] | |||
[[Category: Large Structures]] | |||
[[Category: Shimizu S]] | |||
[[Category: Takenaka A]] | |||
Latest revision as of 12:39, 10 January 2024
The unique structure of wild type carbonic anhydrase alpha-CA1 from Chlamydomonas reinhardtii
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