4enw: Difference between revisions

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==Structure of the S234N variant of E. coli KatE==
==Structure of the S234N variant of E. coli KatE==
<StructureSection load='4enw' size='340' side='right' caption='[[4enw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4enw' size='340' side='right' caption='[[4enw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4enw]] is a 4 chain structure with sequence from [http://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=4ENW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ENW FirstGlance]. <br>
<table><tr><td colspan='2'>[[4enw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ENW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ENW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4enp|4enp]], [[4enq|4enq]], [[4enr|4enr]], [[4ens|4ens]], [[4ent|4ent]], [[4enu|4enu]], [[4env|4env]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4enp|4enp]], [[4enq|4enq]], [[4enr|4enr]], [[4ens|4ens]], [[4ent|4ent]], [[4enu|4enu]], [[4env|4env]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1732, JW1721, katE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1732, JW1721, katE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>
<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=4enw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4enw RCSB], [http://www.ebi.ac.uk/pdbsum/4enw PDBsum]</span></td></tr>
<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=4enw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enw OCA], [http://pdbe.org/4enw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4enw RCSB], [http://www.ebi.ac.uk/pdbsum/4enw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4enw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4enw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Escherichia coli k-12]]
[[Category: Ecoli]]
[[Category: Jha, V]]
[[Category: Jha, V]]
[[Category: Loewen, P C]]
[[Category: Loewen, P C]]

Revision as of 18:14, 5 August 2016

Structure of the S234N variant of E. coli KatEStructure of the S234N variant of E. coli KatE

Structural highlights

4enw is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:b1732, JW1721, katE (ECOLI)
Activity:Catalase, with EC number 1.11.1.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CATE_ECOLI] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Jha V, Chelikani P, Carpena X, Fita I, Loewen PC. Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli. Arch Biochem Biophys. 2012 Oct 1;526(1):54-9. doi: 10.1016/j.abb.2012.06.010., Epub 2012 Jul 20. PMID:22820098 doi:http://dx.doi.org/10.1016/j.abb.2012.06.010

4enw, resolution 1.90Å

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