5b5x

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<StructureSection load='5b5x' size='340' side='right'caption='[[5b5x]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
<StructureSection load='5b5x' size='340' side='right'caption='[[5b5x]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b5x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B5X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b5x]] is a 1 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=5B5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B5X FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.511&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k5w|5k5w]], [[5b5y|5b5y]], [[5b5z|5b5z]], [[5b60|5b60]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LciC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5x OCA], [https://pdbe.org/5b5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b5x RCSB], [https://www.ebi.ac.uk/pdbsum/5b5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5x ProSAT]</span></td></tr>
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<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=5b5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5x OCA], [http://pdbe.org/5b5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b5x RCSB], [http://www.ebi.ac.uk/pdbsum/5b5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5x ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q75NZ1_CHLRE Q75NZ1_CHLRE]
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Aquatic microalgae have evolved diverse CO2-concentrating mechanisms (CCMs) to saturate the carboxylase with its substrate, to compensate for the slow kinetics and competing oxygenation reaction of the key photosynthetic CO2-fixing enzyme rubisco. The limiting CO2-inducible B protein (LCIB) is known to be essential for CCM function in Chlamydomonas reinhardtii To assign a function to this previously uncharacterized protein family, we purified and characterized a phylogenetically diverse set of LCIB homologs. Three of the six homologs are functional carbonic anhydrases (CAs). We determined the crystal structures of LCIB and limiting CO2-inducible C protein (LCIC) from C. reinhardtii and a CA-functional homolog from Phaeodactylum tricornutum, all of which harbor motifs bearing close resemblance to the active site of canonical beta-CAs. Our results identify the LCIB family as a previously unidentified group of beta-CAs, and provide a biochemical foundation for their function in the microalgal CCMs.
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Structural insights into the LCIB protein family reveals a new group of beta-carbonic anhydrases.,Jin S, Sun J, Wunder T, Tang D, Cousins AB, Sze SK, Mueller-Cajar O, Gao YG Proc Natl Acad Sci U S A. 2016 Dec 20;113(51):14716-14721. doi:, 10.1073/pnas.1616294113. Epub 2016 Dec 1. PMID:27911826<ref>PMID:27911826</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5b5x" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chlre]]
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[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao, Y]]
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[[Category: Gao Y]]
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[[Category: Jin, S]]
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[[Category: Jin S]]
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[[Category: Mueller-Cajar, O M]]
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[[Category: Mueller-Cajar OM]]
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[[Category: Sun, J]]
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[[Category: Sun J]]
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[[Category: Tang, D]]
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[[Category: Tang D]]
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[[Category: Wunder, T]]
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[[Category: Wunder T]]
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[[Category: Metal binding protein]]
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[[Category: Metalloprotein]]
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Current revision

Crystal structure of limiting CO2-inducible protein LCIC

PDB ID 5b5x

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