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4atj

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(New page: 200px<br /><applet load="4atj" size="450" color="white" frame="true" align="right" spinBox="true" caption="4atj, resolution 2.50&Aring;" /> '''DISTAL HEME POCKET M...)
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[[Image:4atj.gif|left|200px]]<br /><applet load="4atj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4atj, resolution 2.50&Aring;" />
 
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'''DISTAL HEME POCKET MUTANT (H42E) OF RECOMBINANT HORSERADISH PEROXIDASE IN COMPLEX WITH BENZHYDROXAMIC ACID'''<br />
 
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==Overview==
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==DISTAL HEME POCKET MUTANT (H42E) OF RECOMBINANT HORSERADISH PEROXIDASE IN COMPLEX WITH BENZHYDROXAMIC ACID==
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The crystal structures of horseradish peroxidase C (HRPC) active-site, mutants H42E and R38S/H42E co-crystallized with benzhydroxamic acid (BHA), and ferulic acid (FA), respectively, have been solved. The 2.5 A crystal, structure of the H42E-BHA complex reveals that the side-chain O atoms of, Glu42 occupy positions that are very similar to the positions of the two, side-chain N atoms of the distal histidine in the wild-type HRPC-BHA, structure. The mutation disturbs the hydrogen-bonding network extending, from residue 42 to the distal calcium ion and results in the absence of, the water molecule that is usually ligated to this ion in plant, peroxidases. Consequently, the distal calcium ion is six- rather than, seven-coordinated. In the 2.0 A R38S/H42E structure the position of Glu42, is different and no FA is observed in the distal haem pocket. This is a, consequence of the absence of the Arg38 side chain, which limits the, flexibility of the Glu42 side chain and modulates its acidity, making it, unsuitable as a general acid-base catalyst in the reaction cycle. The, water ligated to the distal calcium ion is present, showing that the, wild-type distal hydrogen-bonding network is preserved. These results show, why a glutamic acid residue can substitute for the conserved distal, histidine in HRPC and that Arg38 plays a significant role in controlling, the positioning and ionization state of the residue at position 42., Furthermore, these structures indicate that changes in the distal cavity, are conveyed through the distal hydrogen-bonding network to the distal, calcium site.
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<StructureSection load='4atj' size='340' side='right'caption='[[4atj]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4atj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ATJ FirstGlance]. <br>
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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]] 2.5&#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=BHO:BENZHYDROXAMIC+ACID'>BHO</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=4atj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atj OCA], [https://pdbe.org/4atj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atj RCSB], [https://www.ebi.ac.uk/pdbsum/4atj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PER1A_ARMRU PER1A_ARMRU] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/at/4atj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=4atj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structures of horseradish peroxidase C (HRPC) active-site mutants H42E and R38S/H42E co-crystallized with benzhydroxamic acid (BHA) and ferulic acid (FA), respectively, have been solved. The 2.5 A crystal structure of the H42E-BHA complex reveals that the side-chain O atoms of Glu42 occupy positions that are very similar to the positions of the two side-chain N atoms of the distal histidine in the wild-type HRPC-BHA structure. The mutation disturbs the hydrogen-bonding network extending from residue 42 to the distal calcium ion and results in the absence of the water molecule that is usually ligated to this ion in plant peroxidases. Consequently, the distal calcium ion is six- rather than seven-coordinated. In the 2.0 A R38S/H42E structure the position of Glu42 is different and no FA is observed in the distal haem pocket. This is a consequence of the absence of the Arg38 side chain, which limits the flexibility of the Glu42 side chain and modulates its acidity, making it unsuitable as a general acid-base catalyst in the reaction cycle. The water ligated to the distal calcium ion is present, showing that the wild-type distal hydrogen-bonding network is preserved. These results show why a glutamic acid residue can substitute for the conserved distal histidine in HRPC and that Arg38 plays a significant role in controlling the positioning and ionization state of the residue at position 42. Furthermore, these structures indicate that changes in the distal cavity are conveyed through the distal hydrogen-bonding network to the distal calcium site.
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==About this Structure==
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Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle.,Meno K, Jennings S, Smith AT, Henriksen A, Gajhede M Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1803-12. Epub, 2002 Sep 28. PMID:12351824<ref>PMID:12351824</ref>
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4ATJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana] with CA, HEM and BHO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4ATJ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle., Meno K, Jennings S, Smith AT, Henriksen A, Gajhede M, Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1803-12. Epub, 2002 Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12351824 12351824]
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</div>
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[[Category: Armoracia rusticana]]
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<div class="pdbe-citations 4atj" style="background-color:#fffaf0;"></div>
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[[Category: Peroxidase]]
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[[Category: Single protein]]
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[[Category: Gajhede, M.]]
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[[Category: Henriksen, A.]]
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[[Category: Jennings, S.]]
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[[Category: Meno, K.]]
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[[Category: Smith, A.T.]]
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[[Category: BHO]]
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[[Category: CA]]
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[[Category: HEM]]
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[[Category: heme enzyme]]
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[[Category: mutant]]
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[[Category: oxidoreductase]]
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[[Category: peroxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:25:34 2007''
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==See Also==
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*[[Horseradish peroxidase|Horseradish peroxidase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Armoracia rusticana]]
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[[Category: Large Structures]]
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[[Category: Gajhede M]]
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[[Category: Henriksen A]]
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[[Category: Jennings S]]
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[[Category: Meno K]]
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[[Category: Smith AT]]

Current revision

DISTAL HEME POCKET MUTANT (H42E) OF RECOMBINANT HORSERADISH PEROXIDASE IN COMPLEX WITH BENZHYDROXAMIC ACID

PDB ID 4atj

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