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3tis

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Current revision (08:37, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3tis' size='340' side='right'caption='[[3tis]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3tis' size='340' side='right'caption='[[3tis]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tis]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TIS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tis]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TIS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tio|3tio]]</div></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=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">yrdA, b3279, JW5710 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3tis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tis OCA], [https://pdbe.org/3tis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tis RCSB], [https://www.ebi.ac.uk/pdbsum/3tis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tis 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=3tis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tis OCA], [https://pdbe.org/3tis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tis RCSB], [https://www.ebi.ac.uk/pdbsum/3tis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tis ProSAT]</span></td></tr>
</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/YRDA_ECOLI YRDA_ECOLI]
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The YrdA protein shows high sequence similarity to gamma-class carbonic anhydrase (gamma-CA) proteins and is classified as part of the gamma-CA protein family. However, its function has not been fully elucidated as it lacks several of the conserved residues that are considered to be necessary for gamma-CA catalysis. Interestingly, a homologue of gamma-CA from Methanosarcina thermophila and a beta-carboxysomal gamma-CA from a beta-cyanobacterium have shown that these catalytic residues are not always conserved in gamma-CAs. The crystal structure of YrdA from Escherichia coli (ecYrdA) is reported here in two crystallographic forms. The overall structure of ecYrdA is also similar to those of the gamma-CAs. One loop around the putative catalytic site shows a number of alternative conformations. A His residue (His70) on this loop coordinates with, or is reoriented from, the catalytic Zn(2+) ion; this is similar to the conformations mediated by an Asp residue on the catalytic loops of beta-CA proteins. One Trp residue (Trp171) also adopts two alternative conformations that may be related to the spatial positions of the catalytic loop. Even though significant CA activity could not be detected using purified ecYrdA, these structural features have potential functional implications for gamma-CA-related proteins.
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Structures of the gamma-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch.,Park HM, Park JH, Choi JW, Lee J, Kim BY, Jung CH, Kim JS Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):920-6. Epub 2012 Jul 7. PMID:22868757<ref>PMID:22868757</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 3tis" 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: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chio, J W]]
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[[Category: Chio JW]]
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[[Category: Jung, J H]]
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[[Category: Jung JH]]
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[[Category: Kim, B Y]]
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[[Category: Kim BY]]
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[[Category: Kim, J S]]
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[[Category: Kim JS]]
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[[Category: Lee, J E]]
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[[Category: Lee JE]]
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[[Category: Park, H M]]
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[[Category: Park HM]]
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[[Category: Phosphate binding]]
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[[Category: Transferase]]
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[[Category: Zn biding]]
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Current revision

Crystal structures of yrdA from Escherichia coli, a homologous protein of gamma-class carbonic anhydrases, show possible allosteric conformations

PDB ID 3tis

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