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1x7u

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Revision as of 05:17, 10 September 2015

Crystal structure of the S324T of catalase-peroxidase KatG

Structural highlights

1x7u is a 2 chain structure with sequence from "bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1mwv
Gene:	KatG ("Bacillus pseudomallei" Whitmore 1913)
Activity:	Catalase, with EC number 1.11.1.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[KATG_BURPS] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.^[1]

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

The Ser315Thr variant of the catalase-peroxidase KatG from Mycobacterium tuberculosis imparts resistance to the pro-drug isonicotinic acid hydrazide (isoniazid) through a failure to convert it to the active drug, isonicotinoyl-NAD. The equivalent variant in KatG from Burkholderia pseudomallei, Ser324Thr, has been constructed, revealing catalase and peroxidase activities that are similar to those of the native enzyme. The other activities of the variant protein, including the NADH oxidase, the isoniazid hydrazinolysis and isonicotinoyl-NAD synthase activities are reduced by 60-70%. The crystal structure of the variant differs from that of the native enzyme in having the methyl group of Thr324 situated in the entrance channel to the heme cavity, in a modified water matrix in the entrance channel and heme cavity, in lacking the putative perhydroxy modification on the heme, in the multiple locations of a few side-chains, and in the presence of an apparent perhydroxy modification on the indole nitrogen atom of the active-site Trp111. The position of the methyl group of Thr324 creates a constriction or narrowing of the channel leading to the heme cavity, providing an explanation for the lower reactivity towards isoniazid and the slower rate of isonicotinoyl-NAD synthesis.

Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei.,Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen PC J Mol Biol. 2005 Jan 7;345(1):21-8. PMID:15567407^[2]

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

References

↑ Singh R, Wiseman B, Deemagarn T, Donald LJ, Duckworth HW, Carpena X, Fita I, Loewen PC. Catalase-peroxidases (KatG) exhibit NADH oxidase activity. J Biol Chem. 2004 Oct 8;279(41):43098-106. Epub 2004 Jul 26. PMID:15280362 doi:10.1074/jbc.M406374200
↑ Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen PC. Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei. J Mol Biol. 2005 Jan 7;345(1):21-8. PMID:15567407 doi:http://dx.doi.org/10.1016/j.jmb.2004.10.020

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/1x7u"

@@ Line 2: / Line 2: @@
 <StructureSection load='1x7u' size='340' side='right' caption='[[1x7u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1x7u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X7U 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mwv|1mwv]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KatG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u PDBsum]</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=1x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7u OCA], [http://pdbe.org/1x7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x7u RCSB], [http://www.ebi.ac.uk/pdbsum/1x7u PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/KATG_BURPS KATG_BURPS]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.<ref>PMID:15280362</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1x7u" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Burkholderia pseudomallei]]
+[[Category: Bacillus pseudomallei whitmore 1913]]
 [[Category: Catalase]]
 [[Category: Carpena, X]]

1x7u

From Proteopedia

Revision as of 05:17, 10 September 2015

Crystal structure of the S324T of catalase-peroxidase KatG

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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