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4enq

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4enq]] is a 4 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=4ENQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ENQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4enq]] is a 4 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=4ENQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ENQ 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=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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]] 1.9&#8491;</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=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=4enq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enq OCA], [https://pdbe.org/4enq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4enq RCSB], [https://www.ebi.ac.uk/pdbsum/4enq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4enq 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=4enq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enq OCA], [https://pdbe.org/4enq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4enq RCSB], [https://www.ebi.ac.uk/pdbsum/4enq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4enq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CATE_ECOLI CATE_ECOLI]] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
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[https://www.uniprot.org/uniprot/CATE_ECOLI CATE_ECOLI] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The main channel for H(2)O(2) access to the heme cavity in large subunit catalases is twice as long as in small subunit catalases and is divided into two distinct parts. Like small subunit catalases, the 15A of the channel adjacent to the heme has a predominantly hydrophobic surface with only weak water occupancy, but the next 15A extending to the protein surface is hydrophilic and contains a complex water matrix in multiple passages. At the approximate junction of these two sections are a conserved serine and glutamate that are hydrogen bonded and associated with H(2)O(2) in inactive variants. Mutation of these residues changed the dimensions of the channel, both enlarging and constricting it, and also changed the solvent occupancy in the hydrophobic, inner section of the main channel. Despite these structural changes and the prominent location of the residues in the channel, the variants exhibited less than a 2-fold change in the k(cat) and apparent K(M) kinetic constants. These results reflect the importance of the complex multi-passage structure of the main channel. Surprisingly, mutation of either the serine or glutamate to an aliphatic side chain interfered with heme oxidation to heme d.
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Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli.,Jha V, Chelikani P, Carpena X, Fita I, Loewen PC Arch Biochem Biophys. 2012 Oct 1;526(1):54-9. doi: 10.1016/j.abb.2012.06.010., Epub 2012 Jul 20. PMID:22820098<ref>PMID:22820098</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 4enq" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Catalase 3D structures|Catalase 3D structures]]
*[[Catalase 3D structures|Catalase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of E530D variant E. coli KatE

PDB ID 4enq

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