1i6p: Difference between revisions

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[[Image:1i6p.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)==
|PDB= 1i6p |SIZE=350|CAPTION= <scene name='initialview01'>1i6p</scene>, resolution 2.00&Aring;
<StructureSection load='1i6p' size='340' side='right'caption='[[1i6p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
<table><tr><td colspan='2'>[[1i6p]] is a 1 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=1I6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6P FirstGlance]. <br>
|ACTIVITY= [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]  
</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&#8491;</td></tr>
|GENE= YADF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6p OCA], [https://pdbe.org/1i6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6p RCSB], [https://www.ebi.ac.uk/pdbsum/1i6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAN_ECOLI CAN_ECOLI]  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i6/1i6p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1i6p ConSurf].
<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 (ECCA)'''
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 1i6p" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1I6P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6P OCA].
__TOC__
 
</StructureSection>
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11316870 11316870]
[[Category: Carbonate dehydratase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[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: ZN]]
[[Category: carbonic anhydrase]]
[[Category: crystal structure]]
[[Category: mad phasing]]
[[Category: metalloenzyme]]
[[Category: ph-dependent activity]]
[[Category: zinc coordination]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:46:11 2008''
Retrieved from "https://proteopedia.org/1i6p"