This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3b1b
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3b1b.png|left|200px]] | ||
| - | + | ==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== | ==See Also== | ||
| - | *[[Carbonic anhydrase|Carbonic anhydrase]] | + | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Shimizu S]] |
| - | [[Category: | + | [[Category: Takenaka A]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
The unique structure of wild type carbonic anhydrase alpha-CA1 from Chlamydomonas reinhardtii
| |||||||||||
