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[[Image:1sch.gif|left|200px]]<br />
<applet load="1sch" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sch, resolution 2.56&Aring;" />
'''PEANUT PEROXIDASE'''<br />


==Overview==
==PEANUT PEROXIDASE==
BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent, oxidations. Based on sequence alignments, heme peroxidases have been, divided into three classes. Crystal structures are available for, peroxidases of classes I and II, but until now no structure has been, determined for class III, the classical extracellular plant peroxidases., RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7, A resolution. The helical fold is similar to that of known peroxidase, structures. The 294-residue polypeptide chain is accompanied by a heme and, two calcium ions, and there is some evidence of glycosylation., CONCLUSIONS. This is the first complete structure of a class III, peroxidase and as such should serve as a model for other class III enzymes, including the much-studied horseradish peroxidase. It may also aid in the, interpretation of functional differences between the peroxidase classes., Ten helices conserved in class I and II peroxidases are also found in, peanut peroxidase. Key residues of the heme environment and the location, of two calcium ions are shared with class II peroxidases. Peanut, peroxidase contains three unique helices, two of which contribute to the, substrate access channel leading to the heme edge.
<StructureSection load='1sch' size='340' side='right'caption='[[1sch]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1sch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCH FirstGlance]. <br>
1SCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea] with NAG, CA and HEM 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] Structure known Active Sites: ADC, ADH, APC, APH, BDC, BDH, BPC and BPH. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCH OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sch OCA], [https://pdbe.org/1sch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sch RCSB], [https://www.ebi.ac.uk/pdbsum/1sch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sch ProSAT]</span></td></tr>
The crystal structure of peanut peroxidase., Schuller DJ, Ban N, Huystee RB, McPherson A, Poulos TL, Structure. 1996 Mar 15;4(3):311-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805539 8805539]
</table>
== Function ==
[https://www.uniprot.org/uniprot/PER1_ARAHY PER1_ARAHY] 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.
== 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/sc/1sch_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=1sch ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Arachis hypogaea]]
[[Category: Arachis hypogaea]]
[[Category: Peroxidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Poulos TL]]
[[Category: Poulos, T.L.]]
[[Category: Schuller DJ]]
[[Category: Schuller, D.J.]]
[[Category: CA]]
[[Category: HEM]]
[[Category: NAG]]
[[Category: calcium binding]]
[[Category: glycosylation]]
[[Category: oxidoreductase]]
[[Category: peroxidase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 17:04:15 2007''

Latest revision as of 11:30, 1 May 2024

PEANUT PEROXIDASEPEANUT PEROXIDASE

Structural highlights

1sch is a 2 chain structure with sequence from Arachis hypogaea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.56Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PER1_ARAHY 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1sch, resolution 2.56Å

Drag the structure with the mouse to rotate

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