2ghc

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[[Image:2ghc.gif|left|200px]]
 
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==Conformational mobility in the active site of a heme peroxidase==
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The line below this paragraph, containing "STRUCTURE_2ghc", creates the "Structure Box" on the page.
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<StructureSection load='2ghc' size='340' side='right'caption='[[2ghc]], [[Resolution|resolution]] 1.25&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'>[[2ghc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GHC 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]] 1.25&#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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene></td></tr>
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{{STRUCTURE_2ghc| PDB=2ghc | 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=2ghc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghc OCA], [https://pdbe.org/2ghc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ghc RCSB], [https://www.ebi.ac.uk/pdbsum/2ghc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ghc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q43758_SOYBN Q43758_SOYBN]
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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/gh/2ghc_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=2ghc ConSurf].
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<div style="clear:both"></div>
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'''Conformational mobility in the active site of a heme peroxidase'''
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==See Also==
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*[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]]
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*[[Plasmid segregation protein ParM|Plasmid segregation protein ParM]]
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==Overview==
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__TOC__
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Conformational mobility of the distal histidine residue has been implicated for several different heme peroxidase enzymes, but unambiguous structural evidence is not available. In this work, we present mechanistic, spectroscopic, and structural evidence for peroxide- and ligand-induced conformational mobility of the distal histidine residue (His-42) in a site-directed variant of ascorbate peroxidase (W41A). In this variant, His-42 binds "on" to the heme in the oxidized form, duplicating the active site structure of the cytochromes b but, in contrast to the cytochromes b, is able to swing "off" the iron during catalysis. This conformational flexibility between the on and off forms is fully reversible and is used as a means to overcome the inherently unreactive nature of the on form toward peroxide, so that essentially complete catalytic activity is maintained. Contrary to the widely adopted view of heme enzyme catalysis, these data indicate that strong coordination of the distal histidine to the heme iron does not automatically undermine catalytic activity. The data add a new dimension to our wider appreciation of structure/activity correlations in other heme enzymes.
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</StructureSection>
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==About this Structure==
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2GHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHC OCA].
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==Reference==
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Conformational mobility in the active site of a heme peroxidase., Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL, J Biol Chem. 2006 Aug 25;281(34):24512-20. Epub 2006 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16762924 16762924]
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[[Category: Glycine max]]
[[Category: Glycine max]]
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[[Category: L-ascorbate peroxidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Badyal SK]]
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[[Category: Badyal, S K.]]
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[[Category: Joyce MG]]
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[[Category: Joyce, M G.]]
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[[Category: Moody PC]]
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[[Category: Moody, P C.]]
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[[Category: Raven EL]]
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[[Category: Raven, E L.]]
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[[Category: Sharp KH]]
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[[Category: Sharp, K H.]]
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[[Category: Orthogonal bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:06:31 2008''
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Current revision

Conformational mobility in the active site of a heme peroxidase

PDB ID 2ghc

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