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2v23

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Structure of cytochrome c peroxidase mutant N184R Y36A

Structural highlights

2v23 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Evolutionary Conservation

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

Publication Abstract from PubMed

Isoniazid (INH, isonicotinic acid hydrazine) is one of only two therapeutic agents effective in treating tuberculosis. This prodrug is activated by the heme enzyme catalase peroxidase (KatG) endogenous to Mycobacterium tuberculosis but the mechanism of activation is poorly understood, in part because the binding interaction has not been properly established. The class I peroxidases ascorbate peroxidase (APX) and cytochrome c peroxidase (CcP) have active site structures very similar to KatG and are also capable of activating isoniazid. We report here the first crystal structures of complexes of isoniazid bound to APX and CcP. These are the first structures of isoniazid bound to any activating enzymes. The structures show that isoniazid binds close to the delta-heme edge in both APX and CcP, although the precise binding orientation varies slightly in the two cases. A second binding site for INH is found in APX at the gamma-heme edge close to the established ascorbate binding site, indicating that the gamma-heme edge can also support the binding of aromatic substrates. We also show that in an active site mutant of soybean APX (W41A) INH can bind directly to the heme iron to become an inhibitor and in a different mode when the distal histidine is replaced by alanine (H42A). These structures provide the first unambiguous evidence for the location of the isoniazid binding site in the class I peroxidases and provide rationalization of isoniazid resistance in naturally occurring KatG mutant strains of M. tuberculosis.

The tuberculosis prodrug isoniazid bound to activating peroxidases.,Metcalfe C, Macdonald IK, Murphy EJ, Brown KA, Raven EL, Moody PC J Biol Chem. 2008 Mar 7;283(10):6193-200. Epub 2007 Dec 5. PMID:18056997^[1]

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

References

↑ Metcalfe C, Macdonald IK, Murphy EJ, Brown KA, Raven EL, Moody PC. The tuberculosis prodrug isoniazid bound to activating peroxidases. J Biol Chem. 2008 Mar 7;283(10):6193-200. Epub 2007 Dec 5. PMID:18056997 doi:10.1074/jbc.M707412200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v23"

@@ Line 1: / Line 1: @@
 ==Structure of cytochrome c peroxidase mutant N184R Y36A==
-<StructureSection load='2v23' size='340' side='right' caption='[[2v23]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='2v23' size='340' side='right'caption='[[2v23]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v23]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V23 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V23 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2f|1a2f]], [[1a2g|1a2g]], [[1aa4|1aa4]], [[1ac4|1ac4]], [[1ac8|1ac8]], [[1aeb|1aeb]], [[1aed|1aed]], [[1aee|1aee]], [[1aef|1aef]], [[1aeg|1aeg]], [[1aeh|1aeh]], [[1aej|1aej]], [[1aek|1aek]], [[1aem|1aem]], [[1aen|1aen]], [[1aeo|1aeo]], [[1aeq|1aeq]], [[1aes|1aes]], [[1aet|1aet]], [[1aeu|1aeu]], [[1aev|1aev]], [[1bej|1bej]], [[1bek|1bek]], [[1bem|1bem]], [[1bep|1bep]], [[1beq|1beq]], [[1bes|1bes]], [[1bj9|1bj9]], [[1bva|1bva]], [[1cca|1cca]], [[1ccb|1ccb]], [[1ccc|1ccc]], [[1cce|1cce]], [[1ccg|1ccg]], [[1cci|1cci]], [[1ccj|1ccj]], [[1cck|1cck]], [[1ccl|1ccl]], [[1ccp|1ccp]], [[1cmp|1cmp]], [[1cmq|1cmq]], [[1cmt|1cmt]], [[1cmu|1cmu]], [[1cpd|1cpd]], [[1cpe|1cpe]], [[1cpf|1cpf]], [[1cpg|1cpg]], [[1cyf|1cyf]], [[1dcc|1dcc]], [[1dj1|1dj1]], [[1dj5|1dj5]], [[1ds4|1ds4]], [[1dse|1dse]], [[1dsg|1dsg]], [[1dso|1dso]], [[1dsp|1dsp]], [[1ebe|1ebe]], [[1jci|1jci]], [[1jdr|1jdr]], [[1kok|1kok]], [[1krj|1krj]], [[1kxm|1kxm]], [[1kxn|1kxn]], [[1mk8|1mk8]], [[1mkq|1mkq]], [[1mkr|1mkr]], [[1ml2|1ml2]], [[1ryc|1ryc]], [[1s6v|1s6v]], [[1sdq|1sdq]], [[1sog|1sog]], [[1stq|1stq]], [[1u74|1u74]], [[1u75|1u75]], [[1z53|1z53]], [[1zby|1zby]], [[1zbz|1zbz]], [[2b0z|2b0z]], [[2b10|2b10]], [[2b11|2b11]], [[2b12|2b12]], [[2bcn|2bcn]], [[2ccp|2ccp]], [[2cep|2cep]], [[2cyp|2cyp]], [[2gb8|2gb8]], [[2pcb|2pcb]], [[2pcc|2pcc]], [[3ccp|3ccp]], [[3ccx|3ccx]], [[4ccp|4ccp]], [[4ccx|4ccx]], [[5ccp|5ccp]], [[6ccp|6ccp]], [[7ccp|7ccp]]</td></tr>
+<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></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v23 OCA], [https://pdbe.org/2v23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v23 RCSB], [https://www.ebi.ac.uk/pdbsum/2v23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v23 ProSAT]</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=2v23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v23 OCA], [http://pdbe.org/2v23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v23 RCSB], [http://www.ebi.ac.uk/pdbsum/2v23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v23 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
 == 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/v2/2v23_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v2/2v23_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2v23" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Cytochrome-c peroxidase]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Brown, K A]]
+[[Category: Brown KA]]
-[[Category: Macdonald, I K]]
+[[Category: Macdonald IK]]
-[[Category: Metcalfe, C L]]
+[[Category: Metcalfe CL]]
-[[Category: Moody, P C.E]]
+[[Category: Moody PCE]]
-[[Category: Raven, E L]]
+[[Category: Raven EL]]
-[[Category: Ccp]]
-[[Category: Cytochrome c peroxidase]]
-[[Category: Heme]]
-[[Category: Hydrogen peroxide]]
-[[Category: Inh]]
-[[Category: Iron]]
-[[Category: Isoniazid]]
-[[Category: Metal-binding]]
-[[Category: Mitochondrion]]
-[[Category: Organic radical]]
-[[Category: Oxidoreductase]]
-[[Category: Peroxidase]]
-[[Category: Transit peptide]]

2v23

From Proteopedia

Current revision

Structure of cytochrome c peroxidase mutant N184R Y36A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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