1apx

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[[Image:1apx.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE==
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The line below this paragraph, containing "STRUCTURE_1apx", creates the "Structure Box" on the page.
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<StructureSection load='1apx' size='340' side='right'caption='[[1apx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1apx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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{{STRUCTURE_1apx| PDB=1apx | SCENE= }}
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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=1apx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apx OCA], [https://pdbe.org/1apx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apx RCSB], [https://www.ebi.ac.uk/pdbsum/1apx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/APX1_PEA APX1_PEA] Plays a key role in hydrogen peroxide removal.
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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/ap/1apx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1apx ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE'''
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==See Also==
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*[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of recombinant pea cytosolic ascorbate peroxidase has been refined to an R = 0.19 for data between 8.0 and 2.2 A resolution and magnitude of F &gt; or = 2 sigma(magnitude of F). The refined model consists of four ascorbate peroxidase monomers consisting of 249 residues per monomer assembled into two homodimers, with one heme group per monomer. The ascorbate peroxidase model confirms that the pea cytosolic enzyme is a noncovalent homodimer held together by a series of ionic interactions arranged around the 2-fold noncrystallographic dimer axis. As expected from the high level of sequence identity (33%), the overall fold of the ascorbate peroxidase monomer closely resembles that of cytochrome c peroxidase. The average root mean square differences for 137 helical alpha-carbon atoms between the four ascorbate peroxidase monomers and cytochrome c peroxidase and for 249 topologically equivalent alpha-carbon atoms are 0.9 and 1.3 A, respectively. The active site structures are also the same, including the hydrogen-bonding interactions between the proximal His ligand, a buried Asp residue, and a Trp residue, whose indole ring is parallel to and in contact with the proximal His ligand just under the heme ring. This proximal Trp residue is thought to be the site of free radical formation in cytochrome c peroxidase compound I and is also essential for enzyme activity. The corresponding Trp in ascorbate peroxidase, Trp179, occupies exactly the same position. The most interesting, and possibly functionally important, difference between the two peroxidases is the presence of a cation binding site in ascorbate peroxidase located approximately 8 A from the alpha-carbon atom of Trp179.
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[[Category: Large Structures]]
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==About this Structure==
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1APX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APX OCA].
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==Reference==
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Crystal structure of recombinant pea cytosolic ascorbate peroxidase., Patterson WR, Poulos TL, Biochemistry. 1995 Apr 4;34(13):4331-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7703247 7703247]
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[[Category: L-ascorbate peroxidase]]
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[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: Single protein]]
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[[Category: Patterson WR]]
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[[Category: Patterson, W R.]]
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[[Category: Poulos TL]]
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[[Category: Poulos, T L.]]
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[[Category: Peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:33:59 2008''
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Current revision

CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE

PDB ID 1apx

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