1i6o: Difference between revisions

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<StructureSection load='1i6o' size='340' side='right'caption='[[1i6o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1i6o' size='340' side='right'caption='[[1i6o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1i6o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1I6O FirstGlance]. <br>
<table><tr><td colspan='2'>[[1i6o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6O FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i6p|1i6p]]</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=1i6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6o OCA], [https://pdbe.org/1i6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6o RCSB], [https://www.ebi.ac.uk/pdbsum/1i6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6o ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YADF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1i6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6o OCA], [http://pdbe.org/1i6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i6o RCSB], [http://www.ebi.ac.uk/pdbsum/1i6o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAN_ECOLI CAN_ECOLI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i6o ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i6o ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carbonic anhydrases fall into three distinct evolutionary and structural classes: alpha, beta, and gamma. The beta-class carbonic anhydrases (beta-CAs) are widely distributed among higher plants, simple eukaryotes, eubacteria, and archaea. We have determined the crystal structure of ECCA, a beta-CA from Escherichia coli, to a resolution of 2.0 A. In agreement with the structure of the beta-CA from the chloroplast of the red alga Porphyridium purpureum, the active-site zinc in ECCA is tetrahedrally coordinated by the side chains of four conserved residues. These results confirm the observation of a unique pattern of zinc ligation in at least some beta-CAS: The absence of a water molecule in the inner coordination sphere is inconsistent with known mechanisms of CA activity. ECCA activity is highly pH-dependent in the physiological range, and its expression in yeast complements an oxygen-sensitive phenotype displayed by a beta-CA-deletion strain. The structural and biochemical characterizations of ECCA presented here and the comparisons with other beta-CA structures suggest that ECCA can adopt two distinct conformations displaying widely divergent catalytic rates.
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.,Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY Protein Sci. 2001 May;10(5):911-22. PMID:11316870<ref>PMID:11316870</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i6o" 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>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Carbonate dehydratase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cronk, J D]]
[[Category: Cronk JD]]
[[Category: Cronk, M R]]
[[Category: Cronk MR]]
[[Category: Endrizzi, J A]]
[[Category: Endrizzi JA]]
[[Category: Neill, J W.O]]
[[Category: O'Neill JW]]
[[Category: Zhang, K Y.J]]
[[Category: Zhang KYJ]]
[[Category: Carbonic anhydrase]]
[[Category: Lyase]]
[[Category: Mad phasing]]
[[Category: Metalloenzyme]]
[[Category: Ph-dependent activity]]
[[Category: Zinc coordination]]

Revision as of 07:44, 3 April 2024

CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)

1i6o, resolution 2.20Å

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